Popović, Milica

Link to this page

Authority KeyName Variants
orcid::0000-0002-3681-2153
  • Popović, Milica (37)
Projects
Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima
[L4-2262] Slovenian ARRS research programme Forest Biology, Ecology and Technology [P4-0107]
Slovenia-Belgium ARRS-FWO program [ARRS/N4-0046-5100-1/2015-59] Slovenia-Serbia bilateral ARRS program [BI-RS/16-17-014]
EUFORINNO - European Forest Research and Innovation HTP-GLYCOMET - Methods for high-throughput glycoproteomic analysis
Production, purification and characterization of enzymes and small molecules and their application as soluble or immobilized in food biotechnology, biofuels production and environmental protection Interactions of natural products, their derivatives and coordination compounds with proteins and nucleic acids
[L404318] [L4-4318]
Young Researchers programme FEBS Collaborative and Experimental Scholarship for Central and Eastern Europe
Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research Beneficial effects of dietary bioactive peptides and polyphenols on cardiovascular health in humans
Biological effects, nutritional intake and status of folate and polysaturate fatty acid (PUFA): improvement of nutrition in Serbia Agrobiodiversity and land-use change in Serbia: an integrated biodiversity assessment of key functional groups of arthropods and plant pathogens
Development of new information and communication technologies, based on advanced mathematical methods, with applications in medicine, telecommunications, power systems, protection of national heritage and education

Author's Bibliography

A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population

Tadić, D.; Popović, Milica; Gavrović-Jankulović, Marija; Đurić, Vojislav; Tomić-Špirić, Vesna; Rašković, Sanvila S.; Perić Popadić, Aleksandra

(Elsevier, 2019)

TY  - JOUR
AU  - Tadić, D.
AU  - Popović, Milica
AU  - Gavrović-Jankulović, Marija
AU  - Đurić, Vojislav
AU  - Tomić-Špirić, Vesna
AU  - Rašković, Sanvila S.
AU  - Perić Popadić, Aleksandra
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3728
AB  - Introduction: In the Serbian population allergy to weed pollen is the most common type of pollen-associated allergy, ahead of grass and tree pollens. Besides causing discomfort, allergy to pollen is often associated with rhinitis and asthma. Allergen-specific immunotherapy (ASIT) is the only treatment that can lead to potential long-term immune modification while reducing development of new sensitization and halting disease progression. The aim of the present study is to evaluate the efficacy of sublingual immunotherapy (SLIT) to weeds in the adult patient population using vaccine produced by the local Serbian Torlak Institute for virology, vaccines and serum. Methods: Adult patients with a clinical history of allergic rhinitis with and without asthma were included in the study. IgE-mediated sensitization to grass, tree and weed pollens was confirmed by skin prick testing and/or positive specific IgE. Patients were divided into two groups: patients with allergy to tree and grass pollen and patients with allergy to weeds. All patients received SLIT for three years, either with or without additional symptomatic therapy. Results: Three-year SLIT therapy led to significant improvement in several parameters, including skin-prick reactivity, decrease in specific IgE and use of symptomatic therapy, with mild adverse effects and high patient satisfaction concerning therapy. Conclusion: Three-year SLIT is a safe and efficient treatment option for respiratory allergy to weeds. Further observations in a larger number of patients could provide a better epidemiological evaluation of SLIT, but the positive effects we observed in our study may be considered representative despite the small number of patients.
PB  - Elsevier
T2  - Revue Francaise d'Allergologie
T1  - A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population
VL  - 59
IS  - 7
SP  - 474
EP  - 480
DO  - 10.1016/j.reval.2019.05.006
ER  - 
@article{
author = "Tadić, D. and Popović, Milica and Gavrović-Jankulović, Marija and Đurić, Vojislav and Tomić-Špirić, Vesna and Rašković, Sanvila S. and Perić Popadić, Aleksandra",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3728",
abstract = "Introduction: In the Serbian population allergy to weed pollen is the most common type of pollen-associated allergy, ahead of grass and tree pollens. Besides causing discomfort, allergy to pollen is often associated with rhinitis and asthma. Allergen-specific immunotherapy (ASIT) is the only treatment that can lead to potential long-term immune modification while reducing development of new sensitization and halting disease progression. The aim of the present study is to evaluate the efficacy of sublingual immunotherapy (SLIT) to weeds in the adult patient population using vaccine produced by the local Serbian Torlak Institute for virology, vaccines and serum. Methods: Adult patients with a clinical history of allergic rhinitis with and without asthma were included in the study. IgE-mediated sensitization to grass, tree and weed pollens was confirmed by skin prick testing and/or positive specific IgE. Patients were divided into two groups: patients with allergy to tree and grass pollen and patients with allergy to weeds. All patients received SLIT for three years, either with or without additional symptomatic therapy. Results: Three-year SLIT therapy led to significant improvement in several parameters, including skin-prick reactivity, decrease in specific IgE and use of symptomatic therapy, with mild adverse effects and high patient satisfaction concerning therapy. Conclusion: Three-year SLIT is a safe and efficient treatment option for respiratory allergy to weeds. Further observations in a larger number of patients could provide a better epidemiological evaluation of SLIT, but the positive effects we observed in our study may be considered representative despite the small number of patients.",
publisher = "Elsevier",
journal = "Revue Francaise d'Allergologie",
title = "A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population",
volume = "59",
number = "7",
pages = "474-480",
doi = "10.1016/j.reval.2019.05.006"
}
Tadić, D., Popović, M., Gavrović-Jankulović, M., Đurić, V., Tomić-Špirić, V., Rašković, S. S.,& Perić Popadić, A. (2019). A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population.
Revue Francaise d'Allergologie
Elsevier., 59(7), 474-480.
https://doi.org/10.1016/j.reval.2019.05.006
Tadić D, Popović M, Gavrović-Jankulović M, Đurić V, Tomić-Špirić V, Rašković SS, Perić Popadić A. A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population. Revue Francaise d'Allergologie. 2019;59(7):474-480
Tadić D., Popović Milica, Gavrović-Jankulović Marija, Đurić Vojislav, Tomić-Špirić Vesna, Rašković Sanvila S., Perić Popadić Aleksandra, "A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population" Revue Francaise d'Allergologie, 59, no. 7 (2019):474-480,
https://doi.org/10.1016/j.reval.2019.05.006 .

The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines

Nešić, Andrijana N.; Čavić, Milena; Popović, Milica; Zlatanova, Milena; Pieters, Raymond; Smit, Joost; Gavrović-Jankulović, Marija

(MDPI, 2019)

TY  - JOUR
AU  - Nešić, Andrijana N.
AU  - Čavić, Milena
AU  - Popović, Milica
AU  - Zlatanova, Milena
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Gavrović-Jankulović, Marija
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3799
AB  - Impairment of the intestinal barrier is one of the key events in the initiation of the sensitization process in food allergy. The aim of this study was to explore the effects of kiwifruit allergen Act d 1 on intestinal permeability and tight junction protein (TJP) gene expression in vivo and to explore its potential to activate the NF-ĸB signaling pathway and to regulate expression of epithelial pro-allergenic cytokines. Influences of Act d 1 on TJP gene expression and pro-allergenic cytokines in the mouse intestine was analyzed by qPCR upon allergen administration by oral gavage. The effect on the in vivo intestinal permeability was assessed in ELISA by measuring the translocation of β-lactoglobulin (BLG) into circulation. The capacity of Act d 1 to activate the NF-ĸB pathway was tested in HEK293 cells by fluorescent microscopy and flow cytometry. Administration of Actinidin (Act d 1) increased intestinal permeability to the BLG. This was accompanied by changes in gene expression of TJP mRNA and pro-allergenic cytokines IL-25, IL-33, and thymic stromal lymphopoietin (TSLP) compared to the control. Act d 1 reduced TEER of the HEK293 monolayer, was positive in an NF-ĸB-reporter HEK293 cell assay, and induced secretion of TSLP. These findings shed more light on the molecular events in the sensitization process of kiwifruit but possibly also of other protease food allergens.
PB  - MDPI
T2  - Biomolecules
T1  - The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines
VL  - 9
IS  - 12
SP  - 816
DO  - 10.3390/biom9120816
ER  - 
@article{
author = "Nešić, Andrijana N. and Čavić, Milena and Popović, Milica and Zlatanova, Milena and Pieters, Raymond and Smit, Joost and Gavrović-Jankulović, Marija",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3799",
abstract = "Impairment of the intestinal barrier is one of the key events in the initiation of the sensitization process in food allergy. The aim of this study was to explore the effects of kiwifruit allergen Act d 1 on intestinal permeability and tight junction protein (TJP) gene expression in vivo and to explore its potential to activate the NF-ĸB signaling pathway and to regulate expression of epithelial pro-allergenic cytokines. Influences of Act d 1 on TJP gene expression and pro-allergenic cytokines in the mouse intestine was analyzed by qPCR upon allergen administration by oral gavage. The effect on the in vivo intestinal permeability was assessed in ELISA by measuring the translocation of β-lactoglobulin (BLG) into circulation. The capacity of Act d 1 to activate the NF-ĸB pathway was tested in HEK293 cells by fluorescent microscopy and flow cytometry. Administration of Actinidin (Act d 1) increased intestinal permeability to the BLG. This was accompanied by changes in gene expression of TJP mRNA and pro-allergenic cytokines IL-25, IL-33, and thymic stromal lymphopoietin (TSLP) compared to the control. Act d 1 reduced TEER of the HEK293 monolayer, was positive in an NF-ĸB-reporter HEK293 cell assay, and induced secretion of TSLP. These findings shed more light on the molecular events in the sensitization process of kiwifruit but possibly also of other protease food allergens.",
publisher = "MDPI",
journal = "Biomolecules",
title = "The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines",
volume = "9",
number = "12",
pages = "816",
doi = "10.3390/biom9120816"
}
Nešić, A. N., Čavić, M., Popović, M., Zlatanova, M., Pieters, R., Smit, J.,& Gavrović-Jankulović, M. (2019). The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines.
Biomolecules
MDPI., 9(12), 816.
https://doi.org/10.3390/biom9120816
Nešić AN, Čavić M, Popović M, Zlatanova M, Pieters R, Smit J, Gavrović-Jankulović M. The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines. Biomolecules. 2019;9(12):816
Nešić Andrijana N., Čavić Milena, Popović Milica, Zlatanova Milena, Pieters Raymond, Smit Joost, Gavrović-Jankulović Marija, "The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines" Biomolecules, 9, no. 12 (2019):816,
https://doi.org/10.3390/biom9120816 .
1
3
3

Isolation of anti-extra-cellular vesicle single-domain antibodies by direct panning on vesicle-enriched fractions

Popović, Milica; Mazzega, Elisa; Toffoletto, Barbara; de Marco, Ario

(Biomed Central Ltd, London, 2018)

TY  - JOUR
AU  - Popović, Milica
AU  - Mazzega, Elisa
AU  - Toffoletto, Barbara
AU  - de Marco, Ario
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2069
AB  - Background: The thorough understanding of the physiological and pathological processes mediated by extracellular vesicles (EVs) is challenged by purification methods which are cumbersome, not reproducible, or insufficient to yield homogeneous material. Chromatography based on both ion-exchange and immune-capture can represent an effective method to improve EV purification and successive analysis. Methods: Cell culture supernatant was used as a model sample for assessing the capacity of anion-exchange chromatography to separate distinct EV fractions and to isolate nanobodies by direct panning on whole EVs to recover binders specific for the native conformation of EV-surface epitopes and suitable to develop EV immune-capture reagents. Results: Anion-exchange chromatography of cell culture supernatant separated distinct protein-containing fractions and all of them were positive for CD9, a biomarker associated to some EVs. This suggested the existence of several EV fractions but did not help in separating EVs from other contaminants. We further isolated several nanobodies instrumental for implementing immune-affinity protocols. These were able to immobilize EVs from both cell culture supernatant and biological samples, to be used in ELISA, flow-cytometry, and immune-purification. Conclusions: Here we report the first successful isolation of anti-EV nanobodies for the use in immunoaffinity-based EV capture by panning a phage library directly on partially purified EVs. This achievement paves the way for the application of direct EV panning for the discovery of novel antibody-vesicle surface biomarker pairs and represents the preliminary requirement for the development of selective immune-capture that, in combination with anion-exchange chromatography, can simplify the systematic stratification of EV sub-populations and their individual characterization.
PB  - Biomed Central Ltd, London
T2  - Microbial Cell Factories
T1  - Isolation of anti-extra-cellular vesicle single-domain antibodies by direct panning on vesicle-enriched fractions
VL  - 17
DO  - 10.1186/s12934-017-0856-9
ER  - 
@article{
author = "Popović, Milica and Mazzega, Elisa and Toffoletto, Barbara and de Marco, Ario",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2069",
abstract = "Background: The thorough understanding of the physiological and pathological processes mediated by extracellular vesicles (EVs) is challenged by purification methods which are cumbersome, not reproducible, or insufficient to yield homogeneous material. Chromatography based on both ion-exchange and immune-capture can represent an effective method to improve EV purification and successive analysis. Methods: Cell culture supernatant was used as a model sample for assessing the capacity of anion-exchange chromatography to separate distinct EV fractions and to isolate nanobodies by direct panning on whole EVs to recover binders specific for the native conformation of EV-surface epitopes and suitable to develop EV immune-capture reagents. Results: Anion-exchange chromatography of cell culture supernatant separated distinct protein-containing fractions and all of them were positive for CD9, a biomarker associated to some EVs. This suggested the existence of several EV fractions but did not help in separating EVs from other contaminants. We further isolated several nanobodies instrumental for implementing immune-affinity protocols. These were able to immobilize EVs from both cell culture supernatant and biological samples, to be used in ELISA, flow-cytometry, and immune-purification. Conclusions: Here we report the first successful isolation of anti-EV nanobodies for the use in immunoaffinity-based EV capture by panning a phage library directly on partially purified EVs. This achievement paves the way for the application of direct EV panning for the discovery of novel antibody-vesicle surface biomarker pairs and represents the preliminary requirement for the development of selective immune-capture that, in combination with anion-exchange chromatography, can simplify the systematic stratification of EV sub-populations and their individual characterization.",
publisher = "Biomed Central Ltd, London",
journal = "Microbial Cell Factories",
title = "Isolation of anti-extra-cellular vesicle single-domain antibodies by direct panning on vesicle-enriched fractions",
volume = "17",
doi = "10.1186/s12934-017-0856-9"
}
Popović, M., Mazzega, E., Toffoletto, B.,& de Marco, A. (2018). Isolation of anti-extra-cellular vesicle single-domain antibodies by direct panning on vesicle-enriched fractions.
Microbial Cell Factories
Biomed Central Ltd, London., 17.
https://doi.org/10.1186/s12934-017-0856-9
Popović M, Mazzega E, Toffoletto B, de Marco A. Isolation of anti-extra-cellular vesicle single-domain antibodies by direct panning on vesicle-enriched fractions. Microbial Cell Factories. 2018;17
Popović Milica, Mazzega Elisa, Toffoletto Barbara, de Marco Ario, "Isolation of anti-extra-cellular vesicle single-domain antibodies by direct panning on vesicle-enriched fractions" Microbial Cell Factories, 17 (2018),
https://doi.org/10.1186/s12934-017-0856-9 .
17
16
17

Canonical and selective approaches in exosome purification and their implications for diagnostic accuracy

Popović, Milica; de Marco, Ario

(Ame Publ Co, Shatin, 2018)

TY  - JOUR
AU  - Popović, Milica
AU  - de Marco, Ario
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2138
AB  - Extracellular vesicles (EVs) play a pivotal role in cell to cell signalling in both physiological and pathological conditions. Based on their biogenesis, three main classes of EVs are recognized: exosomes, microvesicles and apoptotic bodies. Exosomes are cell-derived vesicles (EVs) present in many body fluids (blood, urine, milk, cerebrospinal fluid) ranging in size from 30 to 150 nm. Due to their involvement in numerous physiological and pathological events, cell derived exosomes in bodily fluids represent a unique source of clinically relevant and non-invasive biomarkers. Since biomolecule content present in exosomes reflects the state of the parent cell, exosome analysis and characterization may provide valuable information about the presence of aberrant processes in the cells from which they originated. Because of the large and heterogeneous scientific community working with exosomes, several purification strategies have been applied so far, which yield EV fractions largely differing for quantity and quality. Most of the present exosome isolation approaches based on ultracentrifugation (UC), ultrafiltration (UF) or precipitation, are inefficient and hard to standardize, thereby creating low reproducibility in sample quality and potentially misleading results because highly sensitivity downstream analytical techniques, such as mass spectrometry, can detect even minute traces of co-isolated contaminants. Furthermore, loss of certain exosomal fractions during purification process or damage of exosomal membrane integrity can also alter final protein and RNA profiles. As a consequence, there is a strong interest in consensus principles for the exosome purification and the search for reliable methods for selective isolation of EV sub-populations. In the present manuscript, we critically overview the most commonly used techniques used for exosome preparation such as ultracentrifugation, size-based isolation methods, precipitation and immunoaffinity (IA) and their respective applicability for purification of exosomes from clinically relevant samples.
PB  - Ame Publ Co, Shatin
T2  - TRANSLATIONAL CANCER RESEARCH
T1  - Canonical and selective approaches in exosome purification and their implications for diagnostic accuracy
VL  - 7
DO  - 10.21037/tcr.2017.08.44
ER  - 
@article{
author = "Popović, Milica and de Marco, Ario",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2138",
abstract = "Extracellular vesicles (EVs) play a pivotal role in cell to cell signalling in both physiological and pathological conditions. Based on their biogenesis, three main classes of EVs are recognized: exosomes, microvesicles and apoptotic bodies. Exosomes are cell-derived vesicles (EVs) present in many body fluids (blood, urine, milk, cerebrospinal fluid) ranging in size from 30 to 150 nm. Due to their involvement in numerous physiological and pathological events, cell derived exosomes in bodily fluids represent a unique source of clinically relevant and non-invasive biomarkers. Since biomolecule content present in exosomes reflects the state of the parent cell, exosome analysis and characterization may provide valuable information about the presence of aberrant processes in the cells from which they originated. Because of the large and heterogeneous scientific community working with exosomes, several purification strategies have been applied so far, which yield EV fractions largely differing for quantity and quality. Most of the present exosome isolation approaches based on ultracentrifugation (UC), ultrafiltration (UF) or precipitation, are inefficient and hard to standardize, thereby creating low reproducibility in sample quality and potentially misleading results because highly sensitivity downstream analytical techniques, such as mass spectrometry, can detect even minute traces of co-isolated contaminants. Furthermore, loss of certain exosomal fractions during purification process or damage of exosomal membrane integrity can also alter final protein and RNA profiles. As a consequence, there is a strong interest in consensus principles for the exosome purification and the search for reliable methods for selective isolation of EV sub-populations. In the present manuscript, we critically overview the most commonly used techniques used for exosome preparation such as ultracentrifugation, size-based isolation methods, precipitation and immunoaffinity (IA) and their respective applicability for purification of exosomes from clinically relevant samples.",
publisher = "Ame Publ Co, Shatin",
journal = "TRANSLATIONAL CANCER RESEARCH",
title = "Canonical and selective approaches in exosome purification and their implications for diagnostic accuracy",
volume = "7",
doi = "10.21037/tcr.2017.08.44"
}
Popović, M.,& de Marco, A. (2018). Canonical and selective approaches in exosome purification and their implications for diagnostic accuracy.
TRANSLATIONAL CANCER RESEARCH
Ame Publ Co, Shatin., 7.
https://doi.org/10.21037/tcr.2017.08.44
Popović M, de Marco A. Canonical and selective approaches in exosome purification and their implications for diagnostic accuracy. TRANSLATIONAL CANCER RESEARCH. 2018;7
Popović Milica, de Marco Ario, "Canonical and selective approaches in exosome purification and their implications for diagnostic accuracy" TRANSLATIONAL CANCER RESEARCH, 7 (2018),
https://doi.org/10.21037/tcr.2017.08.44 .
8
6
6

Supplementary material for the article: Popovic, M.; Mazzega, E.; Toffoletto, B.; de Marco, A. Isolation of Anti-Extra-Cellular Vesicle Single-Domain Antibodies by Direct Panning on Vesicle-Enriched Fractions. Microbial cell factories 2018, 17 (1), 6. https://doi.org/10.1186/s12934-017-0856-9

Popović, Milica; Mazzega, Elisa; Toffoletto, Barbara; de Marco, Ario

(Biomed Central Ltd, London, 2018)

TY  - BOOK
AU  - Popović, Milica
AU  - Mazzega, Elisa
AU  - Toffoletto, Barbara
AU  - de Marco, Ario
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3233
PB  - Biomed Central Ltd, London
T2  - Microbial Cell Factories
T1  - Supplementary material for the article: Popovic, M.; Mazzega, E.; Toffoletto, B.; de Marco, A. Isolation of Anti-Extra-Cellular Vesicle Single-Domain Antibodies by Direct Panning on Vesicle-Enriched Fractions. Microbial cell factories 2018, 17 (1), 6. https://doi.org/10.1186/s12934-017-0856-9
ER  - 
@book{
author = "Popović, Milica and Mazzega, Elisa and Toffoletto, Barbara and de Marco, Ario",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3233",
publisher = "Biomed Central Ltd, London",
journal = "Microbial Cell Factories",
title = "Supplementary material for the article: Popovic, M.; Mazzega, E.; Toffoletto, B.; de Marco, A. Isolation of Anti-Extra-Cellular Vesicle Single-Domain Antibodies by Direct Panning on Vesicle-Enriched Fractions. Microbial cell factories 2018, 17 (1), 6. https://doi.org/10.1186/s12934-017-0856-9"
}
Popović, M., Mazzega, E., Toffoletto, B.,& de Marco, A. (2018). Supplementary material for the article: Popovic, M.; Mazzega, E.; Toffoletto, B.; de Marco, A. Isolation of Anti-Extra-Cellular Vesicle Single-Domain Antibodies by Direct Panning on Vesicle-Enriched Fractions. Microbial cell factories 2018, 17 (1), 6. https://doi.org/10.1186/s12934-017-0856-9.
Microbial Cell Factories
Biomed Central Ltd, London..
Popović M, Mazzega E, Toffoletto B, de Marco A. Supplementary material for the article: Popovic, M.; Mazzega, E.; Toffoletto, B.; de Marco, A. Isolation of Anti-Extra-Cellular Vesicle Single-Domain Antibodies by Direct Panning on Vesicle-Enriched Fractions. Microbial cell factories 2018, 17 (1), 6. https://doi.org/10.1186/s12934-017-0856-9. Microbial Cell Factories. 2018;
Popović Milica, Mazzega Elisa, Toffoletto Barbara, de Marco Ario, "Supplementary material for the article: Popovic, M.; Mazzega, E.; Toffoletto, B.; de Marco, A. Isolation of Anti-Extra-Cellular Vesicle Single-Domain Antibodies by Direct Panning on Vesicle-Enriched Fractions. Microbial cell factories 2018, 17 (1), 6. https://doi.org/10.1186/s12934-017-0856-9" Microbial Cell Factories (2018)

Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica)

Popović, Milica; Gregori, Marco; Vodnik, Dominik; Ferlan, Mitja; Mrak, Tanja; Straus, Ines; McDowell, Nathan G.; Kraigher, Hojka; de Marco, Ario

(Canadian Science Publishing, Nrc Research Press, Ottawa, 2017)

TY  - JOUR
AU  - Popović, Milica
AU  - Gregori, Marco
AU  - Vodnik, Dominik
AU  - Ferlan, Mitja
AU  - Mrak, Tanja
AU  - Straus, Ines
AU  - McDowell, Nathan G.
AU  - Kraigher, Hojka
AU  - de Marco, Ario
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2546
AB  - Drought is an environmental stress that impacts plant productivity. Projections show both an increase in intense rain events and a reduction in the number of rain days, conditions that leads to increased risk of drought. Consequently, the identification of molecular biomarkers suitable for evaluating the impact of water deprivation conditions on forest plant seedlings is of significant value for monitoring purposes and forest management. In this study, we evaluated a biochemical methodology for the assessment of drought stress coupled with variable soil temperature in European beech (Fagus sylvatica L.) seedlings by analyzing a set of metabolites and enzymes involved in free radical scavenging and cell wall synthesis. The results indicate that the specific activities and isoform profile of superoxide dismutases and glutathione peroxidases together with the variation of phenolic compounds enable discrimination between seedlings with different degrees of photosynthetic activity. This approach represents a promising platform for the assessment of drought stress in forest trees and could serve for enhancing selection and breeding practices, allowing for plants that are more tolerant of abiotic stress.
PB  - Canadian Science Publishing, Nrc Research Press, Ottawa
T2  - Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere
T1  - Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica)
VL  - 47
IS  - 11
SP  - 1517
EP  - 1526
DO  - 10.1139/cjfr-2016-0530
ER  - 
@article{
author = "Popović, Milica and Gregori, Marco and Vodnik, Dominik and Ferlan, Mitja and Mrak, Tanja and Straus, Ines and McDowell, Nathan G. and Kraigher, Hojka and de Marco, Ario",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2546",
abstract = "Drought is an environmental stress that impacts plant productivity. Projections show both an increase in intense rain events and a reduction in the number of rain days, conditions that leads to increased risk of drought. Consequently, the identification of molecular biomarkers suitable for evaluating the impact of water deprivation conditions on forest plant seedlings is of significant value for monitoring purposes and forest management. In this study, we evaluated a biochemical methodology for the assessment of drought stress coupled with variable soil temperature in European beech (Fagus sylvatica L.) seedlings by analyzing a set of metabolites and enzymes involved in free radical scavenging and cell wall synthesis. The results indicate that the specific activities and isoform profile of superoxide dismutases and glutathione peroxidases together with the variation of phenolic compounds enable discrimination between seedlings with different degrees of photosynthetic activity. This approach represents a promising platform for the assessment of drought stress in forest trees and could serve for enhancing selection and breeding practices, allowing for plants that are more tolerant of abiotic stress.",
publisher = "Canadian Science Publishing, Nrc Research Press, Ottawa",
journal = "Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere",
title = "Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica)",
volume = "47",
number = "11",
pages = "1517-1526",
doi = "10.1139/cjfr-2016-0530"
}
Popović, M., Gregori, M., Vodnik, D., Ferlan, M., Mrak, T., Straus, I., McDowell, N. G., Kraigher, H.,& de Marco, A. (2017). Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica).
Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere
Canadian Science Publishing, Nrc Research Press, Ottawa., 47(11), 1517-1526.
https://doi.org/10.1139/cjfr-2016-0530
Popović M, Gregori M, Vodnik D, Ferlan M, Mrak T, Straus I, McDowell NG, Kraigher H, de Marco A. Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica). Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere. 2017;47(11):1517-1526
Popović Milica, Gregori Marco, Vodnik Dominik, Ferlan Mitja, Mrak Tanja, Straus Ines, McDowell Nathan G., Kraigher Hojka, de Marco Ario, "Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica)" Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere, 47, no. 11 (2017):1517-1526,
https://doi.org/10.1139/cjfr-2016-0530 .
1
1
1
1

Effect of urolithins on oxidative stress of colorectal adenocarcinomacells-Caco-2

Kojadinovic, Milica; Arsic, Aleksandra; Petovic-Oggiano, Gordana; Gavrović-Jankulović, Marija; Glibetic, Marija; Popović, Milica

(Taylor & Francis Ltd, Abingdon, 2017)

TY  - JOUR
AU  - Kojadinovic, Milica
AU  - Arsic, Aleksandra
AU  - Petovic-Oggiano, Gordana
AU  - Gavrović-Jankulović, Marija
AU  - Glibetic, Marija
AU  - Popović, Milica
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2551
AB  - Urolithins (UROs) are metabolites derived from ellagic acid (EA) and ellagitannins (ETs) by gut microbiota after consumption of different ETs. The health effects attributed to UROs are numerous and diverse, ranging from antimalarial properties to anticancer activities and regulation of gene expression. The aim of this work was at assessing the effect of URO-A; -B; -C; -D on the oxidative status of colon epithelium using as a model colorectal adenocarcinoma cell line (Caco-2). No significant cytotoxic effects of UROs was noted, with the applied treatments. Supplementation of cell growth medium with a mixture of UROs decreased the level of intracellular reactive oxygen species both after short- and long-term exposure. UROs also affected the activity of antioxidative enzymes within the cell, especially catalase.Conclusions: At concentrations reached in the lumen of the gut, UROs can exert beneficial effects on the cells by decreasing oxidative stress thus preventing the damage caused by reactive oxygen species.
PB  - Taylor & Francis Ltd, Abingdon
T2  - International Journal of Food Sciences and Nutrition
T1  - Effect of urolithins on oxidative stress of colorectal adenocarcinomacells-Caco-2
VL  - 68
IS  - 8
SP  - 952
EP  - 959
DO  - 10.1080/09637486.2017.1328665
ER  - 
@article{
author = "Kojadinovic, Milica and Arsic, Aleksandra and Petovic-Oggiano, Gordana and Gavrović-Jankulović, Marija and Glibetic, Marija and Popović, Milica",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2551",
abstract = "Urolithins (UROs) are metabolites derived from ellagic acid (EA) and ellagitannins (ETs) by gut microbiota after consumption of different ETs. The health effects attributed to UROs are numerous and diverse, ranging from antimalarial properties to anticancer activities and regulation of gene expression. The aim of this work was at assessing the effect of URO-A; -B; -C; -D on the oxidative status of colon epithelium using as a model colorectal adenocarcinoma cell line (Caco-2). No significant cytotoxic effects of UROs was noted, with the applied treatments. Supplementation of cell growth medium with a mixture of UROs decreased the level of intracellular reactive oxygen species both after short- and long-term exposure. UROs also affected the activity of antioxidative enzymes within the cell, especially catalase.Conclusions: At concentrations reached in the lumen of the gut, UROs can exert beneficial effects on the cells by decreasing oxidative stress thus preventing the damage caused by reactive oxygen species.",
publisher = "Taylor & Francis Ltd, Abingdon",
journal = "International Journal of Food Sciences and Nutrition",
title = "Effect of urolithins on oxidative stress of colorectal adenocarcinomacells-Caco-2",
volume = "68",
number = "8",
pages = "952-959",
doi = "10.1080/09637486.2017.1328665"
}
Kojadinovic, M., Arsic, A., Petovic-Oggiano, G., Gavrović-Jankulović, M., Glibetic, M.,& Popović, M. (2017). Effect of urolithins on oxidative stress of colorectal adenocarcinomacells-Caco-2.
International Journal of Food Sciences and Nutrition
Taylor & Francis Ltd, Abingdon., 68(8), 952-959.
https://doi.org/10.1080/09637486.2017.1328665
Kojadinovic M, Arsic A, Petovic-Oggiano G, Gavrović-Jankulović M, Glibetic M, Popović M. Effect of urolithins on oxidative stress of colorectal adenocarcinomacells-Caco-2. International Journal of Food Sciences and Nutrition. 2017;68(8):952-959
Kojadinovic Milica, Arsic Aleksandra, Petovic-Oggiano Gordana, Gavrović-Jankulović Marija, Glibetic Marija, Popović Milica, "Effect of urolithins on oxidative stress of colorectal adenocarcinomacells-Caco-2" International Journal of Food Sciences and Nutrition, 68, no. 8 (2017):952-959,
https://doi.org/10.1080/09637486.2017.1328665 .
7
6
6

Use of monolithic supports for high-throughput protein and peptide separation in proteomics

Anđelković, Uroš; Tufegdžić, Srđan; Popović, Milica

(Wiley, Hoboken, 2017)

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Tufegdžić, Srđan
AU  - Popović, Milica
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2557
AB  - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
PB  - Wiley, Hoboken
T2  - Electrophoresis
T1  - Use of monolithic supports for high-throughput protein and peptide separation in proteomics
VL  - 38
IS  - 22-23
SP  - 2851
EP  - 2869
DO  - 10.1002/elps.201700221
ER  - 
@article{
author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2557",
abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.",
publisher = "Wiley, Hoboken",
journal = "Electrophoresis",
title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics",
volume = "38",
number = "22-23",
pages = "2851-2869",
doi = "10.1002/elps.201700221"
}
Anđelković, U., Tufegdžić, S.,& Popović, M. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics.
Electrophoresis
Wiley, Hoboken., 38(22-23), 2851-2869.
https://doi.org/10.1002/elps.201700221
Anđelković U, Tufegdžić S, Popović M. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. Electrophoresis. 2017;38(22-23):2851-2869
Anđelković Uroš, Tufegdžić Srđan, Popović Milica, "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" Electrophoresis, 38, no. 22-23 (2017):2851-2869,
https://doi.org/10.1002/elps.201700221 .
6
14
6

Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica)

Popović, Milica; Gregori, Marco; Vodnik, Dominik; Ferlan, Mitja; Mrak, Tanja; Straus, Ines; McDowell, Nathan G.; Kraigher, Hojka; de Marco, Ario

(Canadian Science Publishing, Nrc Research Press, Ottawa, 2017)

TY  - JOUR
AU  - Popović, Milica
AU  - Gregori, Marco
AU  - Vodnik, Dominik
AU  - Ferlan, Mitja
AU  - Mrak, Tanja
AU  - Straus, Ines
AU  - McDowell, Nathan G.
AU  - Kraigher, Hojka
AU  - de Marco, Ario
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2973
AB  - Drought is an environmental stress that impacts plant productivity. Projections show both an increase in intense rain events and a reduction in the number of rain days, conditions that leads to increased risk of drought. Consequently, the identification of molecular biomarkers suitable for evaluating the impact of water deprivation conditions on forest plant seedlings is of significant value for monitoring purposes and forest management. In this study, we evaluated a biochemical methodology for the assessment of drought stress coupled with variable soil temperature in European beech (Fagus sylvatica L.) seedlings by analyzing a set of metabolites and enzymes involved in free radical scavenging and cell wall synthesis. The results indicate that the specific activities and isoform profile of superoxide dismutases and glutathione peroxidases together with the variation of phenolic compounds enable discrimination between seedlings with different degrees of photosynthetic activity. This approach represents a promising platform for the assessment of drought stress in forest trees and could serve for enhancing selection and breeding practices, allowing for plants that are more tolerant of abiotic stress.
PB  - Canadian Science Publishing, Nrc Research Press, Ottawa
T2  - Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere
T1  - Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica)
VL  - 47
IS  - 11
SP  - 1517
EP  - 1526
DO  - 10.1139/cjfr-2016-0530
ER  - 
@article{
author = "Popović, Milica and Gregori, Marco and Vodnik, Dominik and Ferlan, Mitja and Mrak, Tanja and Straus, Ines and McDowell, Nathan G. and Kraigher, Hojka and de Marco, Ario",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2973",
abstract = "Drought is an environmental stress that impacts plant productivity. Projections show both an increase in intense rain events and a reduction in the number of rain days, conditions that leads to increased risk of drought. Consequently, the identification of molecular biomarkers suitable for evaluating the impact of water deprivation conditions on forest plant seedlings is of significant value for monitoring purposes and forest management. In this study, we evaluated a biochemical methodology for the assessment of drought stress coupled with variable soil temperature in European beech (Fagus sylvatica L.) seedlings by analyzing a set of metabolites and enzymes involved in free radical scavenging and cell wall synthesis. The results indicate that the specific activities and isoform profile of superoxide dismutases and glutathione peroxidases together with the variation of phenolic compounds enable discrimination between seedlings with different degrees of photosynthetic activity. This approach represents a promising platform for the assessment of drought stress in forest trees and could serve for enhancing selection and breeding practices, allowing for plants that are more tolerant of abiotic stress.",
publisher = "Canadian Science Publishing, Nrc Research Press, Ottawa",
journal = "Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere",
title = "Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica)",
volume = "47",
number = "11",
pages = "1517-1526",
doi = "10.1139/cjfr-2016-0530"
}
Popović, M., Gregori, M., Vodnik, D., Ferlan, M., Mrak, T., Straus, I., McDowell, N. G., Kraigher, H.,& de Marco, A. (2017). Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica).
Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere
Canadian Science Publishing, Nrc Research Press, Ottawa., 47(11), 1517-1526.
https://doi.org/10.1139/cjfr-2016-0530
Popović M, Gregori M, Vodnik D, Ferlan M, Mrak T, Straus I, McDowell NG, Kraigher H, de Marco A. Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica). Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere. 2017;47(11):1517-1526
Popović Milica, Gregori Marco, Vodnik Dominik, Ferlan Mitja, Mrak Tanja, Straus Ines, McDowell Nathan G., Kraigher Hojka, de Marco Ario, "Identification of stress biomarkers for drought and increased soil temperature in seedlings of European beech (Fagus sylvatica)" Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere, 47, no. 11 (2017):1517-1526,
https://doi.org/10.1139/cjfr-2016-0530 .
1
1
1
1

Use of monolithic supports for high-throughput protein and peptide separation in proteomics

Anđelković, Uroš; Tufegdžić, Srđan; Popović, Milica

(Wiley, Hoboken, 2017)

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Tufegdžić, Srđan
AU  - Popović, Milica
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2976
AB  - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
PB  - Wiley, Hoboken
T2  - Electrophoresis
T1  - Use of monolithic supports for high-throughput protein and peptide separation in proteomics
VL  - 38
IS  - 22-23
SP  - 2851
EP  - 2869
DO  - 10.1002/elps.201700221
ER  - 
@article{
author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2976",
abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.",
publisher = "Wiley, Hoboken",
journal = "Electrophoresis",
title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics",
volume = "38",
number = "22-23",
pages = "2851-2869",
doi = "10.1002/elps.201700221"
}
Anđelković, U., Tufegdžić, S.,& Popović, M. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics.
Electrophoresis
Wiley, Hoboken., 38(22-23), 2851-2869.
https://doi.org/10.1002/elps.201700221
Anđelković U, Tufegdžić S, Popović M. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. Electrophoresis. 2017;38(22-23):2851-2869
Anđelković Uroš, Tufegdžić Srđan, Popović Milica, "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" Electrophoresis, 38, no. 22-23 (2017):2851-2869,
https://doi.org/10.1002/elps.201700221 .
6
14
6

Banana as a food allergen source

Nikolić, Jasna; Popović, Milica; Gavrović-Jankulović, Marija

(2016)

TY  - CHAP
AU  - Nikolić, Jasna
AU  - Popović, Milica
AU  - Gavrović-Jankulović, Marija
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/314
AB  - Banana is a perennial herbaceous plant widely cultivated in the tropical and subtropical regions. The pulp of the fruit is a rich source of minerals, vitamins, antioxidants, low glycemic carbohydrates, and fiber, and thereby its consumption has beneficial effects on human health. These nutritional values and its pleasant taste induced the introduction of banana fruit into human diet in infancy and also during convalescence. However, in spite of positive health effects, banana fruit has been recognized as an important food allergen source. The clinical manifestations of banana allergy have usually been associated with mild, local symptoms denoted as oral allergy syndrome. However, more severe reactions, as well as cases of anaphylactic reactions to banana fruit have been registered. IgE reactivity of banana is associated with different proteins, and, so far, only six allergens have been identified and characterized: profilin - actin binding protein (Mus a 1), a class 1 chitinase (Mus a 2), non-specific lipid transfer protein (Mus a 3), thaumatin-like protein (Mus a 4), beta-1,3-glucanase (Mus a 5), and recently registered ascorbate peroxidase (Mus a 6). In this review, we will address the structural features of identified banana allergens and correlate in vitro and in vivo clinical reactivity with their structural homologs from other allergen sources. © 2016 Nova Science Publishers, Inc.
T1  - Banana as a food allergen source
SP  - 107
EP  - 126
ER  - 
@article{
author = "Nikolić, Jasna and Popović, Milica and Gavrović-Jankulović, Marija",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/314",
abstract = "Banana is a perennial herbaceous plant widely cultivated in the tropical and subtropical regions. The pulp of the fruit is a rich source of minerals, vitamins, antioxidants, low glycemic carbohydrates, and fiber, and thereby its consumption has beneficial effects on human health. These nutritional values and its pleasant taste induced the introduction of banana fruit into human diet in infancy and also during convalescence. However, in spite of positive health effects, banana fruit has been recognized as an important food allergen source. The clinical manifestations of banana allergy have usually been associated with mild, local symptoms denoted as oral allergy syndrome. However, more severe reactions, as well as cases of anaphylactic reactions to banana fruit have been registered. IgE reactivity of banana is associated with different proteins, and, so far, only six allergens have been identified and characterized: profilin - actin binding protein (Mus a 1), a class 1 chitinase (Mus a 2), non-specific lipid transfer protein (Mus a 3), thaumatin-like protein (Mus a 4), beta-1,3-glucanase (Mus a 5), and recently registered ascorbate peroxidase (Mus a 6). In this review, we will address the structural features of identified banana allergens and correlate in vitro and in vivo clinical reactivity with their structural homologs from other allergen sources. © 2016 Nova Science Publishers, Inc.",
title = "Banana as a food allergen source",
pages = "107-126"
}
Nikolić, J., Popović, M.,& Gavrović-Jankulović, M. (2016). Banana as a food allergen source.
, 107-126.
Nikolić J, Popović M, Gavrović-Jankulović M. Banana as a food allergen source. 2016;:107-126
Nikolić Jasna, Popović Milica, Gavrović-Jankulović Marija, "Banana as a food allergen source" (2016):107-126

Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris)

Popović, Milica; Sustar, Vid; Gricar, Jozica; Straus, Ines; Torkar, Gregor; Kraigher, Hojka; de Marco, Ario

(Canadian Science Publishing, Nrc Research Press, Ottawa, 2016)

TY  - JOUR
AU  - Popović, Milica
AU  - Sustar, Vid
AU  - Gricar, Jozica
AU  - Straus, Ines
AU  - Torkar, Gregor
AU  - Kraigher, Hojka
AU  - de Marco, Ario
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2049
AB  - Climate development models predict alterations that will critically influence plant metabolism in southern and central Europe. Although the molecular players involved in the response to climatic stress factors have been well described in crops, little information is available for forest tree species. Consequently, the identification of molecular biomarkers suitable for evaluating the actual impact of different environmental stress conditions on forest plants would be of great importance for monitoring purposes and forest management. In this study, we evaluated a biochemical methodology for the assessment of temperature stress in European beech (Fagus sylvatica L.) and Scots pine (Pinus sylvestris L.) seedlings by analyzing a set of metabolites and enzymes involved in free radical scavenging and cell wall synthesis. The results indicate that the combined analysis of the specific activities and isoform profile of peroxidases, superoxide dismutases, and glutathione peroxidases coupled with the amount variation of phenolic compounds enabled the discrimination between stressed and control seedlings. This approach represents a promising platform for the assessment of temperature stress in forest trees and could also enhance selection and breeding practices, allowing for plants more tolerant and (or) resistant to abiotic stress.
PB  - Canadian Science Publishing, Nrc Research Press, Ottawa
T2  - Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere
T1  - Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris)
VL  - 46
IS  - 1
SP  - 58
EP  - 66
DO  - 10.1139/cjfr-2015-0274
ER  - 
@article{
author = "Popović, Milica and Sustar, Vid and Gricar, Jozica and Straus, Ines and Torkar, Gregor and Kraigher, Hojka and de Marco, Ario",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2049",
abstract = "Climate development models predict alterations that will critically influence plant metabolism in southern and central Europe. Although the molecular players involved in the response to climatic stress factors have been well described in crops, little information is available for forest tree species. Consequently, the identification of molecular biomarkers suitable for evaluating the actual impact of different environmental stress conditions on forest plants would be of great importance for monitoring purposes and forest management. In this study, we evaluated a biochemical methodology for the assessment of temperature stress in European beech (Fagus sylvatica L.) and Scots pine (Pinus sylvestris L.) seedlings by analyzing a set of metabolites and enzymes involved in free radical scavenging and cell wall synthesis. The results indicate that the combined analysis of the specific activities and isoform profile of peroxidases, superoxide dismutases, and glutathione peroxidases coupled with the amount variation of phenolic compounds enabled the discrimination between stressed and control seedlings. This approach represents a promising platform for the assessment of temperature stress in forest trees and could also enhance selection and breeding practices, allowing for plants more tolerant and (or) resistant to abiotic stress.",
publisher = "Canadian Science Publishing, Nrc Research Press, Ottawa",
journal = "Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere",
title = "Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris)",
volume = "46",
number = "1",
pages = "58-66",
doi = "10.1139/cjfr-2015-0274"
}
Popović, M., Sustar, V., Gricar, J., Straus, I., Torkar, G., Kraigher, H.,& de Marco, A. (2016). Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris).
Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere
Canadian Science Publishing, Nrc Research Press, Ottawa., 46(1), 58-66.
https://doi.org/10.1139/cjfr-2015-0274
Popović M, Sustar V, Gricar J, Straus I, Torkar G, Kraigher H, de Marco A. Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris). Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere. 2016;46(1):58-66
Popović Milica, Sustar Vid, Gricar Jozica, Straus Ines, Torkar Gregor, Kraigher Hojka, de Marco Ario, "Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris)" Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere, 46, no. 1 (2016):58-66,
https://doi.org/10.1139/cjfr-2015-0274 .
1
5
6
6

Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris)

Popović, Milica; Sustar, Vid; Gricar, Jozica; Straus, Ines; Torkar, Gregor; Kraigher, Hojka; de Marco, Ario

(Canadian Science Publishing, Nrc Research Press, Ottawa, 2016)

TY  - JOUR
AU  - Popović, Milica
AU  - Sustar, Vid
AU  - Gricar, Jozica
AU  - Straus, Ines
AU  - Torkar, Gregor
AU  - Kraigher, Hojka
AU  - de Marco, Ario
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3530
AB  - Climate development models predict alterations that will critically influence plant metabolism in southern and central Europe. Although the molecular players involved in the response to climatic stress factors have been well described in crops, little information is available for forest tree species. Consequently, the identification of molecular biomarkers suitable for evaluating the actual impact of different environmental stress conditions on forest plants would be of great importance for monitoring purposes and forest management. In this study, we evaluated a biochemical methodology for the assessment of temperature stress in European beech (Fagus sylvatica L.) and Scots pine (Pinus sylvestris L.) seedlings by analyzing a set of metabolites and enzymes involved in free radical scavenging and cell wall synthesis. The results indicate that the combined analysis of the specific activities and isoform profile of peroxidases, superoxide dismutases, and glutathione peroxidases coupled with the amount variation of phenolic compounds enabled the discrimination between stressed and control seedlings. This approach represents a promising platform for the assessment of temperature stress in forest trees and could also enhance selection and breeding practices, allowing for plants more tolerant and (or) resistant to abiotic stress.
PB  - Canadian Science Publishing, Nrc Research Press, Ottawa
T2  - Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere
T1  - Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris)
VL  - 46
IS  - 1
SP  - 58
EP  - 66
DO  - 10.1139/cjfr-2015-0274
ER  - 
@article{
author = "Popović, Milica and Sustar, Vid and Gricar, Jozica and Straus, Ines and Torkar, Gregor and Kraigher, Hojka and de Marco, Ario",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3530",
abstract = "Climate development models predict alterations that will critically influence plant metabolism in southern and central Europe. Although the molecular players involved in the response to climatic stress factors have been well described in crops, little information is available for forest tree species. Consequently, the identification of molecular biomarkers suitable for evaluating the actual impact of different environmental stress conditions on forest plants would be of great importance for monitoring purposes and forest management. In this study, we evaluated a biochemical methodology for the assessment of temperature stress in European beech (Fagus sylvatica L.) and Scots pine (Pinus sylvestris L.) seedlings by analyzing a set of metabolites and enzymes involved in free radical scavenging and cell wall synthesis. The results indicate that the combined analysis of the specific activities and isoform profile of peroxidases, superoxide dismutases, and glutathione peroxidases coupled with the amount variation of phenolic compounds enabled the discrimination between stressed and control seedlings. This approach represents a promising platform for the assessment of temperature stress in forest trees and could also enhance selection and breeding practices, allowing for plants more tolerant and (or) resistant to abiotic stress.",
publisher = "Canadian Science Publishing, Nrc Research Press, Ottawa",
journal = "Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere",
title = "Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris)",
volume = "46",
number = "1",
pages = "58-66",
doi = "10.1139/cjfr-2015-0274"
}
Popović, M., Sustar, V., Gricar, J., Straus, I., Torkar, G., Kraigher, H.,& de Marco, A. (2016). Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris).
Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere
Canadian Science Publishing, Nrc Research Press, Ottawa., 46(1), 58-66.
https://doi.org/10.1139/cjfr-2015-0274
Popović M, Sustar V, Gricar J, Straus I, Torkar G, Kraigher H, de Marco A. Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris). Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere. 2016;46(1):58-66
Popović Milica, Sustar Vid, Gricar Jozica, Straus Ines, Torkar Gregor, Kraigher Hojka, de Marco Ario, "Identification of environmental stress biomarkers in seedlings of European beech (Fagus sylvatica) and Scots pine (Pinus sylvestris)" Canadian Journal of Forest Research = Revue Canadienne de La Recherche Forestiere, 46, no. 1 (2016):58-66,
https://doi.org/10.1139/cjfr-2015-0274 .
1
5
6
6

Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage

Rašković, Brankica; Popović, Milica; Ostojić, Sanja B.; Anđelković, Boban D.; Tešević, Vele; Polović, Natalija

(Pergamon-Elsevier Science Ltd, Oxford, 2015)

TY  - JOUR
AU  - Rašković, Brankica
AU  - Popović, Milica
AU  - Ostojić, Sanja B.
AU  - Anđelković, Boban D.
AU  - Tešević, Vele
AU  - Polović, Natalija
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3367
AB  - Papain is a cysteine protease with wide substrate specificity and many applications. Despite its widespread applications, cold stability of papain has never been studied. Here, we used differential spectroscopy to monitor thermal denaturation process. Papain was the most stabile from 45 degrees C to 60 degrees C with Delta G degrees(321) of 13.9 +/- 0.3 kJ/mol and T-m value of 84 +/- 1 degrees C. After cold storage, papain lost parts of its native secondary structures elements which gave an increase of 40% of intermolecular beta-sheet content (band maximum detected at frequency of 1621 cm(-1) in Fourier transform infrared (FT-IR) spectrum) indicating the presence of secondary structures necessary for aggregation. The presence of protein aggregates after cold storage was also proven by analytical size exclusion chromatography. After six freeze-thaw cycles around 75% of starting enzyme activity of papain was lost due to cold denaturation and aggregation of unfolded protein. Autoproteolysis of papain did not cause significant loss of the protein activity. Upon the cold storage, papain underwent structural rearrangements and aggregation that correspond to other cold denatured proteins, rather than autoproteolysis which could have the commercial importance for the growing polypeptide based industry.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy
T1  - Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage
VL  - 150
SP  - 238
EP  - 246
DO  - 10.1016/j.saa.2015.05.061
ER  - 
@article{
author = "Rašković, Brankica and Popović, Milica and Ostojić, Sanja B. and Anđelković, Boban D. and Tešević, Vele and Polović, Natalija",
year = "2015",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3367",
abstract = "Papain is a cysteine protease with wide substrate specificity and many applications. Despite its widespread applications, cold stability of papain has never been studied. Here, we used differential spectroscopy to monitor thermal denaturation process. Papain was the most stabile from 45 degrees C to 60 degrees C with Delta G degrees(321) of 13.9 +/- 0.3 kJ/mol and T-m value of 84 +/- 1 degrees C. After cold storage, papain lost parts of its native secondary structures elements which gave an increase of 40% of intermolecular beta-sheet content (band maximum detected at frequency of 1621 cm(-1) in Fourier transform infrared (FT-IR) spectrum) indicating the presence of secondary structures necessary for aggregation. The presence of protein aggregates after cold storage was also proven by analytical size exclusion chromatography. After six freeze-thaw cycles around 75% of starting enzyme activity of papain was lost due to cold denaturation and aggregation of unfolded protein. Autoproteolysis of papain did not cause significant loss of the protein activity. Upon the cold storage, papain underwent structural rearrangements and aggregation that correspond to other cold denatured proteins, rather than autoproteolysis which could have the commercial importance for the growing polypeptide based industry.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy",
title = "Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage",
volume = "150",
pages = "238-246",
doi = "10.1016/j.saa.2015.05.061"
}
Rašković, B., Popović, M., Ostojić, S. B., Anđelković, B. D., Tešević, V.,& Polović, N. (2015). Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage.
Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy
Pergamon-Elsevier Science Ltd, Oxford., 150, 238-246.
https://doi.org/10.1016/j.saa.2015.05.061
Rašković B, Popović M, Ostojić SB, Anđelković BD, Tešević V, Polović N. Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage. Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy. 2015;150:238-246
Rašković Brankica, Popović Milica, Ostojić Sanja B., Anđelković Boban D., Tešević Vele, Polović Natalija, "Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage" Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy, 150 (2015):238-246,
https://doi.org/10.1016/j.saa.2015.05.061 .
17
17
19

Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage

Rašković, Brankica; Popović, Milica; Ostojić, Sanja B.; Anđelković, Boban D.; Tešević, Vele; Polović, Natalija

(Pergamon-Elsevier Science Ltd, Oxford, 2015)

TY  - JOUR
AU  - Rašković, Brankica
AU  - Popović, Milica
AU  - Ostojić, Sanja B.
AU  - Anđelković, Boban D.
AU  - Tešević, Vele
AU  - Polović, Natalija
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1970
AB  - Papain is a cysteine protease with wide substrate specificity and many applications. Despite its widespread applications, cold stability of papain has never been studied. Here, we used differential spectroscopy to monitor thermal denaturation process. Papain was the most stabile from 45 degrees C to 60 degrees C with Delta G degrees(321) of 13.9 +/- 0.3 kJ/mol and T-m value of 84 +/- 1 degrees C. After cold storage, papain lost parts of its native secondary structures elements which gave an increase of 40% of intermolecular beta-sheet content (band maximum detected at frequency of 1621 cm(-1) in Fourier transform infrared (FT-IR) spectrum) indicating the presence of secondary structures necessary for aggregation. The presence of protein aggregates after cold storage was also proven by analytical size exclusion chromatography. After six freeze-thaw cycles around 75% of starting enzyme activity of papain was lost due to cold denaturation and aggregation of unfolded protein. Autoproteolysis of papain did not cause significant loss of the protein activity. Upon the cold storage, papain underwent structural rearrangements and aggregation that correspond to other cold denatured proteins, rather than autoproteolysis which could have the commercial importance for the growing polypeptide based industry.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy
T1  - Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage
VL  - 150
SP  - 238
EP  - 246
DO  - 10.1016/j.saa.2015.05.061
ER  - 
@article{
author = "Rašković, Brankica and Popović, Milica and Ostojić, Sanja B. and Anđelković, Boban D. and Tešević, Vele and Polović, Natalija",
year = "2015",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1970",
abstract = "Papain is a cysteine protease with wide substrate specificity and many applications. Despite its widespread applications, cold stability of papain has never been studied. Here, we used differential spectroscopy to monitor thermal denaturation process. Papain was the most stabile from 45 degrees C to 60 degrees C with Delta G degrees(321) of 13.9 +/- 0.3 kJ/mol and T-m value of 84 +/- 1 degrees C. After cold storage, papain lost parts of its native secondary structures elements which gave an increase of 40% of intermolecular beta-sheet content (band maximum detected at frequency of 1621 cm(-1) in Fourier transform infrared (FT-IR) spectrum) indicating the presence of secondary structures necessary for aggregation. The presence of protein aggregates after cold storage was also proven by analytical size exclusion chromatography. After six freeze-thaw cycles around 75% of starting enzyme activity of papain was lost due to cold denaturation and aggregation of unfolded protein. Autoproteolysis of papain did not cause significant loss of the protein activity. Upon the cold storage, papain underwent structural rearrangements and aggregation that correspond to other cold denatured proteins, rather than autoproteolysis which could have the commercial importance for the growing polypeptide based industry.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy",
title = "Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage",
volume = "150",
pages = "238-246",
doi = "10.1016/j.saa.2015.05.061"
}
Rašković, B., Popović, M., Ostojić, S. B., Anđelković, B. D., Tešević, V.,& Polović, N. (2015). Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage.
Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy
Pergamon-Elsevier Science Ltd, Oxford., 150, 238-246.
https://doi.org/10.1016/j.saa.2015.05.061
Rašković B, Popović M, Ostojić SB, Anđelković BD, Tešević V, Polović N. Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage. Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy. 2015;150:238-246
Rašković Brankica, Popović Milica, Ostojić Sanja B., Anđelković Boban D., Tešević Vele, Polović Natalija, "Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage" Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy, 150 (2015):238-246,
https://doi.org/10.1016/j.saa.2015.05.061 .
17
17
19

Yeast surface display is a novel tool for the rapid immunological characterization of plant-derived food allergens

Popović, Milica; Prodanović, Radivoje; Ostafe, Raluca; Schillberg, Stefan; Fischer, Rainer; Gavrović-Jankulović, Marija

(Humana Press Inc, Totowa, 2015)

TY  - JOUR
AU  - Popović, Milica
AU  - Prodanović, Radivoje
AU  - Ostafe, Raluca
AU  - Schillberg, Stefan
AU  - Fischer, Rainer
AU  - Gavrović-Jankulović, Marija
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1668
AB  - High-throughput characterization of allergens relies often on phage display technique which is subject to the limitations of a prokaryotic expression system. Substituting the phage display platform with a yeast surface display could lead to fast immunological characterization of allergens with complex structures. Our objective was to evaluate the potential of yeast surface display for characterization of plant-derived food allergens. The coding sequence of mature actinidin (Act d 1) was cloned into pCTCON2 surface display vector. Flow cytometry was used to confirm localization of recombinant Act d 1 on the surface of yeast cells using rabbit polyclonal antisera IgG and IgE from sera of kiwifruit-allergic individuals. Immunological (dot blot, immunoblot ELISA and ELISA inhibition), biochemical (enzymatic activity in gel) and biological (basophil activation) characterization of Act d 1 after solubilization from the yeast cell confirmed that recombinant Act d 1 produced on the surface of yeast cell is similar to its natural counterpart isolated from green kiwifruit. Yeast surface display is a potent technique that enables fast immunochemical characterization of allergens in situ without the need for protein purification and offers an alternative that could lead to improvement of standard immunodiagnostic and immunotherapeutic approaches.
PB  - Humana Press Inc, Totowa
T2  - Immunologic Research
T1  - Yeast surface display is a novel tool for the rapid immunological characterization of plant-derived food allergens
VL  - 61
IS  - 3
SP  - 230
EP  - 239
DO  - 10.1007/s12026-014-8614-0
ER  - 
@article{
author = "Popović, Milica and Prodanović, Radivoje and Ostafe, Raluca and Schillberg, Stefan and Fischer, Rainer and Gavrović-Jankulović, Marija",
year = "2015",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1668",
abstract = "High-throughput characterization of allergens relies often on phage display technique which is subject to the limitations of a prokaryotic expression system. Substituting the phage display platform with a yeast surface display could lead to fast immunological characterization of allergens with complex structures. Our objective was to evaluate the potential of yeast surface display for characterization of plant-derived food allergens. The coding sequence of mature actinidin (Act d 1) was cloned into pCTCON2 surface display vector. Flow cytometry was used to confirm localization of recombinant Act d 1 on the surface of yeast cells using rabbit polyclonal antisera IgG and IgE from sera of kiwifruit-allergic individuals. Immunological (dot blot, immunoblot ELISA and ELISA inhibition), biochemical (enzymatic activity in gel) and biological (basophil activation) characterization of Act d 1 after solubilization from the yeast cell confirmed that recombinant Act d 1 produced on the surface of yeast cell is similar to its natural counterpart isolated from green kiwifruit. Yeast surface display is a potent technique that enables fast immunochemical characterization of allergens in situ without the need for protein purification and offers an alternative that could lead to improvement of standard immunodiagnostic and immunotherapeutic approaches.",
publisher = "Humana Press Inc, Totowa",
journal = "Immunologic Research",
title = "Yeast surface display is a novel tool for the rapid immunological characterization of plant-derived food allergens",
volume = "61",
number = "3",
pages = "230-239",
doi = "10.1007/s12026-014-8614-0"
}
Popović, M., Prodanović, R., Ostafe, R., Schillberg, S., Fischer, R.,& Gavrović-Jankulović, M. (2015). Yeast surface display is a novel tool for the rapid immunological characterization of plant-derived food allergens.
Immunologic Research
Humana Press Inc, Totowa., 61(3), 230-239.
https://doi.org/10.1007/s12026-014-8614-0
Popović M, Prodanović R, Ostafe R, Schillberg S, Fischer R, Gavrović-Jankulović M. Yeast surface display is a novel tool for the rapid immunological characterization of plant-derived food allergens. Immunologic Research. 2015;61(3):230-239
Popović Milica, Prodanović Radivoje, Ostafe Raluca, Schillberg Stefan, Fischer Rainer, Gavrović-Jankulović Marija, "Yeast surface display is a novel tool for the rapid immunological characterization of plant-derived food allergens" Immunologic Research, 61, no. 3 (2015):230-239,
https://doi.org/10.1007/s12026-014-8614-0 .
1
5
4
4

Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy

Grozdanovic, M.; Popović, Milica; Gavrović-Jankulović, Marija

(2014)

TY  - CHAP
AU  - Grozdanovic, M.
AU  - Popović, Milica
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/294
AB  - Persons suffering from allergy (Type I hypersensitivity) produce immunoglobulin E against innocuous environmental antigens such as pollen, house dust, animal dander, food proteins. Diagnosis of allergy is based on the measurement of allergen-specific IgE antibodies and on provocation with allergens in skin prick test. Diagnostic reagents based on allergen extracts obtained from natural biological material often reveal unbalanced allergen content, a presence of nonallergenic components, and are difficult to standardize. Replacement of allergen extracts with a set of individual allergens in component-resolved diagnostics is regarded as a tool for patient selection for specific immunotherapy. The concept of using single recombinant allergens to determine the patient's sensitization profile was coined "component-resolved diagnosis" and is regarded as a precondition for patient-tailored immunotherapy, i.e.,"component resolved immunotherapy"To provide reliable, more specific reagents for allergy diagnosis and therapy recombinant DNA technology has been widely applied. The majority of recombinant allergens by far, have been produced in the prokaryotic expression system; however eukaryotic cells (yeast, plant, insect and mammalian cells) were also exploited. To avoid side effects in the course of immunotherapy various approaches in design of hypoallergenic molecules have been performed. This chapter will give an overview of the concepts and approaches in producing recombinant allergens for component resolved diagnosis and component resolved immunotherapy. © 2014 by Nova Science Publishers, Inc. All rights reserved.
T1  - Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy
VL  - 11
SP  - 19
EP  - 46
ER  - 
@article{
author = "Grozdanovic, M. and Popović, Milica and Gavrović-Jankulović, Marija",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/294",
abstract = "Persons suffering from allergy (Type I hypersensitivity) produce immunoglobulin E against innocuous environmental antigens such as pollen, house dust, animal dander, food proteins. Diagnosis of allergy is based on the measurement of allergen-specific IgE antibodies and on provocation with allergens in skin prick test. Diagnostic reagents based on allergen extracts obtained from natural biological material often reveal unbalanced allergen content, a presence of nonallergenic components, and are difficult to standardize. Replacement of allergen extracts with a set of individual allergens in component-resolved diagnostics is regarded as a tool for patient selection for specific immunotherapy. The concept of using single recombinant allergens to determine the patient's sensitization profile was coined "component-resolved diagnosis" and is regarded as a precondition for patient-tailored immunotherapy, i.e.,"component resolved immunotherapy"To provide reliable, more specific reagents for allergy diagnosis and therapy recombinant DNA technology has been widely applied. The majority of recombinant allergens by far, have been produced in the prokaryotic expression system; however eukaryotic cells (yeast, plant, insect and mammalian cells) were also exploited. To avoid side effects in the course of immunotherapy various approaches in design of hypoallergenic molecules have been performed. This chapter will give an overview of the concepts and approaches in producing recombinant allergens for component resolved diagnosis and component resolved immunotherapy. © 2014 by Nova Science Publishers, Inc. All rights reserved.",
title = "Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy",
volume = "11",
pages = "19-46"
}
Grozdanovic, M., Popović, M.,& Gavrović-Jankulović, M. (2014). Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy.
, 11, 19-46.
Grozdanovic M, Popović M, Gavrović-Jankulović M. Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy. 2014;11:19-46
Grozdanovic M., Popović Milica, Gavrović-Jankulović Marija, "Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy", 11 (2014):19-46

Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein

Prokopovic, Vladimir; Popović, Milica; Anđelković, Uroš; Marsavelski, Aleksandra; Rašković, Brankica; Gavrović-Jankulović, Marija; Polović, Natalija

(Pergamon-Elsevier Science Ltd, Oxford, 2014)

TY  - JOUR
AU  - Prokopovic, Vladimir
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Marsavelski, Aleksandra
AU  - Rašković, Brankica
AU  - Gavrović-Jankulović, Marija
AU  - Polović, Natalija
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1520
AB  - Objective: Human BPIFA2 (parotid secretory protein) is a ubiquitous soluble salivary protein, which belongs to the PLUNC family of proteins. Having sequence similarity to bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein, PLUNC proteins are probably involved in local antibacterial response at mucosal sites, such as oral cavity. The aim of the study was to isolate and characterize human BPIFA2. Design: In this paper, we report one-step affinity chromatography method for BPIFA2 purification from whole human saliva. The isolated BPIFA2 was identified by trypsin mass fingerprinting and characterized by electrophoretic methods. Antibacterial activity of BPIFA2 against model microorganism Pseudomonas aeruginosa was shown in minimum inhibitory concentration and time kill study assays. Results: The protein showed microheterogeneity, both in molecular weight and pI value. BPIFA2 inhibited the growth of P. aeruginosa in microgram concentration range determined by minimum inhibitory concentration assay. In the time kill study, 32 mu g/mL BPIFA2 showed clear bactericidal activity and did not cause any aggregation of bacteria. Conclusion: Affinity chromatography is well suited for isolation of functional BPIFA2 with a potent bactericidal activity against P. aeruginosa. (C) 2013 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Archives of Oral Biology
T1  - Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein
VL  - 59
IS  - 3
SP  - 302
EP  - 309
DO  - 10.1016/j.archoralbio.2013.12.005
ER  - 
@article{
author = "Prokopovic, Vladimir and Popović, Milica and Anđelković, Uroš and Marsavelski, Aleksandra and Rašković, Brankica and Gavrović-Jankulović, Marija and Polović, Natalija",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1520",
abstract = "Objective: Human BPIFA2 (parotid secretory protein) is a ubiquitous soluble salivary protein, which belongs to the PLUNC family of proteins. Having sequence similarity to bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein, PLUNC proteins are probably involved in local antibacterial response at mucosal sites, such as oral cavity. The aim of the study was to isolate and characterize human BPIFA2. Design: In this paper, we report one-step affinity chromatography method for BPIFA2 purification from whole human saliva. The isolated BPIFA2 was identified by trypsin mass fingerprinting and characterized by electrophoretic methods. Antibacterial activity of BPIFA2 against model microorganism Pseudomonas aeruginosa was shown in minimum inhibitory concentration and time kill study assays. Results: The protein showed microheterogeneity, both in molecular weight and pI value. BPIFA2 inhibited the growth of P. aeruginosa in microgram concentration range determined by minimum inhibitory concentration assay. In the time kill study, 32 mu g/mL BPIFA2 showed clear bactericidal activity and did not cause any aggregation of bacteria. Conclusion: Affinity chromatography is well suited for isolation of functional BPIFA2 with a potent bactericidal activity against P. aeruginosa. (C) 2013 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Archives of Oral Biology",
title = "Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein",
volume = "59",
number = "3",
pages = "302-309",
doi = "10.1016/j.archoralbio.2013.12.005"
}
Prokopovic, V., Popović, M., Anđelković, U., Marsavelski, A., Rašković, B., Gavrović-Jankulović, M.,& Polović, N. (2014). Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein.
Archives of Oral Biology
Pergamon-Elsevier Science Ltd, Oxford., 59(3), 302-309.
https://doi.org/10.1016/j.archoralbio.2013.12.005
Prokopovic V, Popović M, Anđelković U, Marsavelski A, Rašković B, Gavrović-Jankulović M, Polović N. Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein. Archives of Oral Biology. 2014;59(3):302-309
Prokopovic Vladimir, Popović Milica, Anđelković Uroš, Marsavelski Aleksandra, Rašković Brankica, Gavrović-Jankulović Marija, Polović Natalija, "Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein" Archives of Oral Biology, 59, no. 3 (2014):302-309,
https://doi.org/10.1016/j.archoralbio.2013.12.005 .
14
12
10

Protocol for simultaneous isolation of three important banana allergens

Nikolić, Jasna; Mrkić, Ivan; Grozdanović, Milica; Popović, Milica; Petersen, Arnd; Jappe, Uta; Gavrović-Jankulović, Marija

(Elsevier Science Bv, Amsterdam, 2014)

TY  - JOUR
AU  - Nikolić, Jasna
AU  - Mrkić, Ivan
AU  - Grozdanović, Milica
AU  - Popović, Milica
AU  - Petersen, Arnd
AU  - Jappe, Uta
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1804
AB  - Banana fruit (Musa acuminata) has become an important food allergen source in recent years. So far, 5 IgE reactive banana proteins have been identified, and the major allergens are: Mus a 2 (a class I chitinase, 31 kDa),Mus a4 (thaumatin-like protein, 21 kDa), and Mus a 5 (beta-1,3-glucanase,33 kDa). Due to variations in allergen expression levels, diagnostic reagents for food allergy can be improved by using individual allergen components instead of banana allergen extracts. The purpose of this study was to optimize the purification protocol of the three major allergens present in banana fruit: Mus a 2, Mus a 4 and Mus a 5. By employing a three-step purification protocol (a combination of anion-exchange, cation-exchange and reversed-phase chromatography) three important banana allergens were obtained in sufficient yield and high purity. Characterization of the purified proteins was performed by both biochemical (2-D PAGE, mass fingerprint and N-terminal sequencing) and immunochemical (immunoblot) methods. IgE reactivity to the purified allergens was tested by employing sera of five allergic patients. The purified allergens displayed higher sensitivity in IgE detection than the routinely used extracts. The three purified allergens are good candidates for reagents in component-based diagnosis of banana allergy. (C) 2014 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Chromatography B: Analytical Technologies in the Biomedical and L
T1  - Protocol for simultaneous isolation of three important banana allergens
VL  - 962
SP  - 30
EP  - 36
DO  - 10.1016/j.jchromb.2014.05.020
ER  - 
@article{
author = "Nikolić, Jasna and Mrkić, Ivan and Grozdanović, Milica and Popović, Milica and Petersen, Arnd and Jappe, Uta and Gavrović-Jankulović, Marija",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1804",
abstract = "Banana fruit (Musa acuminata) has become an important food allergen source in recent years. So far, 5 IgE reactive banana proteins have been identified, and the major allergens are: Mus a 2 (a class I chitinase, 31 kDa),Mus a4 (thaumatin-like protein, 21 kDa), and Mus a 5 (beta-1,3-glucanase,33 kDa). Due to variations in allergen expression levels, diagnostic reagents for food allergy can be improved by using individual allergen components instead of banana allergen extracts. The purpose of this study was to optimize the purification protocol of the three major allergens present in banana fruit: Mus a 2, Mus a 4 and Mus a 5. By employing a three-step purification protocol (a combination of anion-exchange, cation-exchange and reversed-phase chromatography) three important banana allergens were obtained in sufficient yield and high purity. Characterization of the purified proteins was performed by both biochemical (2-D PAGE, mass fingerprint and N-terminal sequencing) and immunochemical (immunoblot) methods. IgE reactivity to the purified allergens was tested by employing sera of five allergic patients. The purified allergens displayed higher sensitivity in IgE detection than the routinely used extracts. The three purified allergens are good candidates for reagents in component-based diagnosis of banana allergy. (C) 2014 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Chromatography B: Analytical Technologies in the Biomedical and L",
title = "Protocol for simultaneous isolation of three important banana allergens",
volume = "962",
pages = "30-36",
doi = "10.1016/j.jchromb.2014.05.020"
}
Nikolić, J., Mrkić, I., Grozdanović, M., Popović, M., Petersen, A., Jappe, U.,& Gavrović-Jankulović, M. (2014). Protocol for simultaneous isolation of three important banana allergens.
Journal of Chromatography B: Analytical Technologies in the Biomedical and L
Elsevier Science Bv, Amsterdam., 962, 30-36.
https://doi.org/10.1016/j.jchromb.2014.05.020
Nikolić J, Mrkić I, Grozdanović M, Popović M, Petersen A, Jappe U, Gavrović-Jankulović M. Protocol for simultaneous isolation of three important banana allergens. Journal of Chromatography B: Analytical Technologies in the Biomedical and L. 2014;962:30-36
Nikolić Jasna, Mrkić Ivan, Grozdanović Milica, Popović Milica, Petersen Arnd, Jappe Uta, Gavrović-Jankulović Marija, "Protocol for simultaneous isolation of three important banana allergens" Journal of Chromatography B: Analytical Technologies in the Biomedical and L, 962 (2014):30-36,
https://doi.org/10.1016/j.jchromb.2014.05.020 .
1
9
8
10

Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)

Popović, Milica; Anđelković, Uroš; Burazer, Lidija M.; Lindner, Buko; Petersen, Arnd; Gavrović-Jankulović, Marija

(Pergamon-Elsevier Science Ltd, Oxford, 2013)

TY  - JOUR
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Burazer, Lidija M.
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1403
AB  - Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 mu g/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling post-harvest diseases and maintaining food quality.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Phytochemistry
T1  - Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)
VL  - 94
SP  - 53
EP  - 59
DO  - 10.1016/j.phytochem.2013.06.006
ER  - 
@article{
author = "Popović, Milica and Anđelković, Uroš and Burazer, Lidija M. and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1403",
abstract = "Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 mu g/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling post-harvest diseases and maintaining food quality.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Phytochemistry",
title = "Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)",
volume = "94",
pages = "53-59",
doi = "10.1016/j.phytochem.2013.06.006"
}
Popović, M., Anđelković, U., Burazer, L. M., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M. (2013). Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa).
Phytochemistry
Pergamon-Elsevier Science Ltd, Oxford., 94, 53-59.
https://doi.org/10.1016/j.phytochem.2013.06.006
Popović M, Anđelković U, Burazer LM, Lindner B, Petersen A, Gavrović-Jankulović M. Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). Phytochemistry. 2013;94:53-59
Popović Milica, Anđelković Uroš, Burazer Lidija M., Lindner Buko, Petersen Arnd, Gavrović-Jankulović Marija, "Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)" Phytochemistry, 94 (2013):53-59,
https://doi.org/10.1016/j.phytochem.2013.06.006 .
1
16
16
17

In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)

Popović, Milica; Anđelković, Uroš; Grozdanović, Milica; Aleksić, Ivana; Gavrović-Jankulović, Marija

(Springer, New York, 2013)

TY  - JOUR
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Grozdanović, Milica
AU  - Aleksić, Ivana
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1612
AB  - The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.
PB  - Springer, New York
T2  - Indian Journal of Microbiology
T1  - In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)
VL  - 53
IS  - 1
SP  - 100
EP  - 105
DO  - 10.1007/s12088-012-0319-2
ER  - 
@article{
author = "Popović, Milica and Anđelković, Uroš and Grozdanović, Milica and Aleksić, Ivana and Gavrović-Jankulović, Marija",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1612",
abstract = "The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.",
publisher = "Springer, New York",
journal = "Indian Journal of Microbiology",
title = "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)",
volume = "53",
number = "1",
pages = "100-105",
doi = "10.1007/s12088-012-0319-2"
}
Popović, M., Anđelković, U., Grozdanović, M., Aleksić, I.,& Gavrović-Jankulović, M. (2013). In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa).
Indian Journal of Microbiology
Springer, New York., 53(1), 100-105.
https://doi.org/10.1007/s12088-012-0319-2
Popović M, Anđelković U, Grozdanović M, Aleksić I, Gavrović-Jankulović M. In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa). Indian Journal of Microbiology. 2013;53(1):100-105
Popović Milica, Anđelković Uroš, Grozdanović Milica, Aleksić Ivana, Gavrović-Jankulović Marija, "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)" Indian Journal of Microbiology, 53, no. 1 (2013):100-105,
https://doi.org/10.1007/s12088-012-0319-2 .
9
9
10

Kiwifruit as a food allergen source

Popović, Milica; Grozdanović, Milica; Gavrović-Jankulović, Marija

(Serbian Chemical Soc, Belgrade, 2013)

TY  - JOUR
AU  - Popović, Milica
AU  - Grozdanović, Milica
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1623
AB  - Since its first appearance on the market, kiwifruit has become very popular in the human diet due to its pleasant taste, low caloric value and high content of vitamin C. However, kiwifruit allergy has become a frequent cause of type I hypersensitivity in the western society. The molecular basis for kiwifruit allergy has been ascribed to up-to-now 11 identified IgE reactive molecules. They are proteins and glycoproteins with a molecular mass between 10 and 50 kDa. The major kiwifruit allergen is a cysteine protease denoted as Act d 1, which represents 50 % of the soluble protein extract. Due to differences in the abundance of the protein components and biological activity, the quality of kiwifruit extracts intended for allergy diagnosis can vary in content and amount of IgE reactive molecules. In addition, the quality of allergen extracts for allergy diagnosis depends on the fruit ripening stage and storage conditions. In terms of clinical reactivity, it has become evident that kiwifruit allergy is not a homogeneous disorder. Different patterns of IgE reactivity accompany several clinical subgroups that have been identified in different geographical regions. In the last decade, enormous progress has been made in the isolation and characterization of kiwifruit allergens. This paper presents an overview of the structural features of kiwifruit allergens.
AB  - Od prvog pojavljivanja na tržištu plod kivija je postao izuzetno popularan sastojak humane ishrane usled prijatnog ukusa, niske kalorijske vrednosti i visokog sadržaja vitamina C. Međutim, alergija na kivi je postala učestali uzrok preosetljivosti tipa I u zapadnom društvu. Do sada je otkriveno 11 IgE vezujućih molekula koji čine molekulsku osnovu alergije na kivi. To su proteini i glikoproteini molekulskih masa između 10 i 50 kDa. Glavni alergen kivija je cistein-proteaza označena kao Act d 1, koja sačinjava 50 % rastvornih proteina ploda kivija. Usled razlike u zastupljenosti proteinskih komponenti i biološkoj aktivnosti, kvalitet proteinskih ekstrakata kivija koji se upotrebljavaju u dijagnostifikovanju alergije može varirati u sadržaju i količini IgE reaktivnih molekula. Takođe, kvalitet alergenih ekstrakata zavisi od stepena zrelosti voća prilikom branja, kao i od uslova skladištenja voća nakon branja. Po pitanju kliničke reaktivnosti postalo je očigledno da alergija na plod kivija ne predstavlja homogeni poremećaj. Različiti obrasci IgE reaktivnosti uočeni su kod nekolicine kliničkih podgrupa koje su identifikovane u različitim geografskim regijama. Tokom poslednje decenije načinjen je veliki napredak u izolovanju i karakterizaciji IgE vezujućih proteina kivija. U okviru ovog rada daćemo pregled strukturnih osobina alergenih proteina kivija.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Kiwifruit as a food allergen source
T1  - Plod kivija kao izvor alergena hrane
VL  - 78
IS  - 3
SP  - 333
EP  - 352
DO  - 10.2298/JSC121210011P
ER  - 
@article{
author = "Popović, Milica and Grozdanović, Milica and Gavrović-Jankulović, Marija",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1623",
abstract = "Since its first appearance on the market, kiwifruit has become very popular in the human diet due to its pleasant taste, low caloric value and high content of vitamin C. However, kiwifruit allergy has become a frequent cause of type I hypersensitivity in the western society. The molecular basis for kiwifruit allergy has been ascribed to up-to-now 11 identified IgE reactive molecules. They are proteins and glycoproteins with a molecular mass between 10 and 50 kDa. The major kiwifruit allergen is a cysteine protease denoted as Act d 1, which represents 50 % of the soluble protein extract. Due to differences in the abundance of the protein components and biological activity, the quality of kiwifruit extracts intended for allergy diagnosis can vary in content and amount of IgE reactive molecules. In addition, the quality of allergen extracts for allergy diagnosis depends on the fruit ripening stage and storage conditions. In terms of clinical reactivity, it has become evident that kiwifruit allergy is not a homogeneous disorder. Different patterns of IgE reactivity accompany several clinical subgroups that have been identified in different geographical regions. In the last decade, enormous progress has been made in the isolation and characterization of kiwifruit allergens. This paper presents an overview of the structural features of kiwifruit allergens., Od prvog pojavljivanja na tržištu plod kivija je postao izuzetno popularan sastojak humane ishrane usled prijatnog ukusa, niske kalorijske vrednosti i visokog sadržaja vitamina C. Međutim, alergija na kivi je postala učestali uzrok preosetljivosti tipa I u zapadnom društvu. Do sada je otkriveno 11 IgE vezujućih molekula koji čine molekulsku osnovu alergije na kivi. To su proteini i glikoproteini molekulskih masa između 10 i 50 kDa. Glavni alergen kivija je cistein-proteaza označena kao Act d 1, koja sačinjava 50 % rastvornih proteina ploda kivija. Usled razlike u zastupljenosti proteinskih komponenti i biološkoj aktivnosti, kvalitet proteinskih ekstrakata kivija koji se upotrebljavaju u dijagnostifikovanju alergije može varirati u sadržaju i količini IgE reaktivnih molekula. Takođe, kvalitet alergenih ekstrakata zavisi od stepena zrelosti voća prilikom branja, kao i od uslova skladištenja voća nakon branja. Po pitanju kliničke reaktivnosti postalo je očigledno da alergija na plod kivija ne predstavlja homogeni poremećaj. Različiti obrasci IgE reaktivnosti uočeni su kod nekolicine kliničkih podgrupa koje su identifikovane u različitim geografskim regijama. Tokom poslednje decenije načinjen je veliki napredak u izolovanju i karakterizaciji IgE vezujućih proteina kivija. U okviru ovog rada daćemo pregled strukturnih osobina alergenih proteina kivija.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Kiwifruit as a food allergen source, Plod kivija kao izvor alergena hrane",
volume = "78",
number = "3",
pages = "333-352",
doi = "10.2298/JSC121210011P"
}
Popović, M., Grozdanović, M.,& Gavrović-Jankulović, M. (2013). Plod kivija kao izvor alergena hrane.
Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 78(3), 333-352.
https://doi.org/10.2298/JSC121210011P
Popović M, Grozdanović M, Gavrović-Jankulović M. Plod kivija kao izvor alergena hrane. Journal of the Serbian Chemical Society. 2013;78(3):333-352
Popović Milica, Grozdanović Milica, Gavrović-Jankulović Marija, "Plod kivija kao izvor alergena hrane" Journal of the Serbian Chemical Society, 78, no. 3 (2013):333-352,
https://doi.org/10.2298/JSC121210011P .
7
5
6

Optimization of the heterologous expression of banana glucanase in Escherichia coli

Abughren, Mohamed; Popović, Milica; Dimitrijevic, Rajna; Burazer, Lidija M.; Grozdanović, Milica; Atanasković-Marković, Marina; Gavrović-Jankulović, Marija

(Serbian Chemical Soc, Belgrade, 2012)

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica
AU  - Dimitrijevic, Rajna
AU  - Burazer, Lidija M.
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1246
AB  - For the heterologous production of a banana glucanase in Escherichia coli, its gene (GenBank GQ268963) was cloned into a pGEX-4T expression vector as a fusion protein with glutathione-S-transferase (GST). BL21 cells transformed with the GST-Mus a 5 construct were employed for production of the protein induced by 1 mM isopropyl-beta-D-thiogalactopyranoside (IPTG). The conditions for protein expression were optimized by varying the temperature (25, 30 and 37 C) and duration of protein expression (3, 6 and 12 h). The level of protein production was analyzed by densitometry of the sodium dodecyl sulfate-polyacrylamide gel (SDS-PAG) after electrophoretic resolution of the respective cell lysates. The optimal protein expression for downstream processing was obtained after 12 h of cell growth at 25 degrees C upon addition of IPTG. Recombinant GST-Mus a 5 purified by glutathione affinity chromatography revealed a molecular mass of about 60 kDa. The IgE and IgG reactivity of the rGST-Mus a 5 was confirmed by dot blot analysis with sera of individual patients from subjects with banana allergy and polyclonal rabbit antibodies against banana extract, respectively. The purified recombinant glucanase is a potential candidate for banana allergy diagnosis.
AB  - Za potrebe proizvodnje u Escherichia coli gen glukanaze iz banane (GenBank GQ268963) je ukloniran u ekspresioni vektor pGEX-4T sa glutation-S-transferazom (GST). Proizvodnja ovog proteina u ćelijama je indukovana 1 mM izopropil-β-D-tiogalaktopiranozidom (IPTG). Uslovi za ekspresiju proteina su optimizovani variranjem temperature (25, 30 i 37°C) i dužine trajanja proteinske sinteze (3, 6 i 12 h). Nivo proizvodnje proteina je analiziran denzitometrijom SDS-PA gela nakon elektroforetskog razdvajanja ćelijskih lizata. Optimalna proizvodnja proteina za njegovo dalje procesovanje je dobijena gajenjem ćelija nakon dodatka IPTG na 25°C tokom 12 h. Rekombinantni GST-Mus a 5 prečišćen afinitetnom hromatografijom sa glutationom pokazuje molekulsku masu od 60 kDa. IgE i IgG reaktivnost izolovane glukanaze potvrđena je u 'dot blot' sa pojedinačnim serumima osoba alergičnih na bananu, i sa poliklonskim zečijim antitelima na ekstrakt banane, redom. Prečišćena rekombinantna glukanaza je potencijalan kandidat za dijagnozu alergije na bananu.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Optimization of the heterologous expression of banana glucanase in Escherichia coli
T1  - Optimizacija heterologe proizvodnje glukanaze iz banane u E. coli
VL  - 77
IS  - 1
SP  - 43
EP  - 52
DO  - 10.2298/JSC110309158A
ER  - 
@article{
author = "Abughren, Mohamed and Popović, Milica and Dimitrijevic, Rajna and Burazer, Lidija M. and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1246",
abstract = "For the heterologous production of a banana glucanase in Escherichia coli, its gene (GenBank GQ268963) was cloned into a pGEX-4T expression vector as a fusion protein with glutathione-S-transferase (GST). BL21 cells transformed with the GST-Mus a 5 construct were employed for production of the protein induced by 1 mM isopropyl-beta-D-thiogalactopyranoside (IPTG). The conditions for protein expression were optimized by varying the temperature (25, 30 and 37 C) and duration of protein expression (3, 6 and 12 h). The level of protein production was analyzed by densitometry of the sodium dodecyl sulfate-polyacrylamide gel (SDS-PAG) after electrophoretic resolution of the respective cell lysates. The optimal protein expression for downstream processing was obtained after 12 h of cell growth at 25 degrees C upon addition of IPTG. Recombinant GST-Mus a 5 purified by glutathione affinity chromatography revealed a molecular mass of about 60 kDa. The IgE and IgG reactivity of the rGST-Mus a 5 was confirmed by dot blot analysis with sera of individual patients from subjects with banana allergy and polyclonal rabbit antibodies against banana extract, respectively. The purified recombinant glucanase is a potential candidate for banana allergy diagnosis., Za potrebe proizvodnje u Escherichia coli gen glukanaze iz banane (GenBank GQ268963) je ukloniran u ekspresioni vektor pGEX-4T sa glutation-S-transferazom (GST). Proizvodnja ovog proteina u ćelijama je indukovana 1 mM izopropil-β-D-tiogalaktopiranozidom (IPTG). Uslovi za ekspresiju proteina su optimizovani variranjem temperature (25, 30 i 37°C) i dužine trajanja proteinske sinteze (3, 6 i 12 h). Nivo proizvodnje proteina je analiziran denzitometrijom SDS-PA gela nakon elektroforetskog razdvajanja ćelijskih lizata. Optimalna proizvodnja proteina za njegovo dalje procesovanje je dobijena gajenjem ćelija nakon dodatka IPTG na 25°C tokom 12 h. Rekombinantni GST-Mus a 5 prečišćen afinitetnom hromatografijom sa glutationom pokazuje molekulsku masu od 60 kDa. IgE i IgG reaktivnost izolovane glukanaze potvrđena je u 'dot blot' sa pojedinačnim serumima osoba alergičnih na bananu, i sa poliklonskim zečijim antitelima na ekstrakt banane, redom. Prečišćena rekombinantna glukanaza je potencijalan kandidat za dijagnozu alergije na bananu.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Optimization of the heterologous expression of banana glucanase in Escherichia coli, Optimizacija heterologe proizvodnje glukanaze iz banane u E. coli",
volume = "77",
number = "1",
pages = "43-52",
doi = "10.2298/JSC110309158A"
}
Abughren, M., Popović, M., Dimitrijevic, R., Burazer, L. M., Grozdanović, M., Atanasković-Marković, M.,& Gavrović-Jankulović, M. (2012). Optimizacija heterologe proizvodnje glukanaze iz banane u E. coli.
Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 77(1), 43-52.
https://doi.org/10.2298/JSC110309158A
Abughren M, Popović M, Dimitrijevic R, Burazer LM, Grozdanović M, Atanasković-Marković M, Gavrović-Jankulović M. Optimizacija heterologe proizvodnje glukanaze iz banane u E. coli. Journal of the Serbian Chemical Society. 2012;77(1):43-52
Abughren Mohamed, Popović Milica, Dimitrijevic Rajna, Burazer Lidija M., Grozdanović Milica, Atanasković-Marković Marina, Gavrović-Jankulović Marija, "Optimizacija heterologe proizvodnje glukanaze iz banane u E. coli" Journal of the Serbian Chemical Society, 77, no. 1 (2012):43-52,
https://doi.org/10.2298/JSC110309158A .
1
2
2

Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)

Abughren, Mohamed; Popović, Milica; Dimitrijevic, Rajna; Burazer, Lidija M.; Grozdanović, Milica; Atanasković-Marković, Marina; Gavrović-Jankulović, Marija

(Serbian Chemical Soc, Belgrade, 2012)

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica
AU  - Dimitrijevic, Rajna
AU  - Burazer, Lidija M.
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1259
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)
VL  - 77
IS  - 2
SP  - 257
EP  - 258
ER  - 
@article{
author = "Abughren, Mohamed and Popović, Milica and Dimitrijevic, Rajna and Burazer, Lidija M. and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1259",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)",
volume = "77",
number = "2",
pages = "257-258"
}
Abughren, M., Popović, M., Dimitrijevic, R., Burazer, L. M., Grozdanović, M., Atanasković-Marković, M.,& Gavrović-Jankulović, M. (2012). Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012).
Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 77(2), 257-258.
Abughren M, Popović M, Dimitrijevic R, Burazer LM, Grozdanović M, Atanasković-Marković M, Gavrović-Jankulović M. Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012). Journal of the Serbian Chemical Society. 2012;77(2):257-258
Abughren Mohamed, Popović Milica, Dimitrijevic Rajna, Burazer Lidija M., Grozdanović Milica, Atanasković-Marković Marina, Gavrović-Jankulović Marija, "Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)" Journal of the Serbian Chemical Society, 77, no. 2 (2012):257-258

Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy

Grozdanović, Milica; Popović, Milica; Polović, Natalija; Burazer, Lidija M.; Vuckovic, Olga; Atanasković-Marković, Marina; Lindner, Buko; Petersen, Arnd; Gavrović-Jankulović, Marija

(Pergamon-Elsevier Science Ltd, Oxford, 2012)

TY  - JOUR
AU  - Grozdanović, Milica
AU  - Popović, Milica
AU  - Polović, Natalija
AU  - Burazer, Lidija M.
AU  - Vuckovic, Olga
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1286
AB  - Actinidin, an abundant cysteine protease from kiwifruit, is a specific biomarker of isolated allergy to kiwifruit. This study evaluates the IgE-binding properties of biologically active and thermally inactivated actinidin. Employing two different activity assays (caseinolytic assay and zymogram with gelatin) we showed that actinidin obtained from kiwifruit extract under native conditions represents a mixture of inactive and active enzyme. The structural integrity of actinidin was confirmed by SDS-PAGE. Edman degradation, mass fingerprint and Western blot with polyclonal antibodies. Although it was capable of inducing positive skin prick test reactions, we failed to detect IgE reactivity of active actinidin in Western blot with patient sera. Thermally inactivated actinidin exhibited IgE reactivity both in vivo and in vitro, indicating that heat processed kiwifruit products may induce clinical reactivity. These findings imply that apart from the allergenic epitopes on its surface, actinidin also contains hidden epitopes inside the protein which become accessible to IgE upon thermal treatment. (C) 2011 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Food and Chemical Toxicology
T1  - Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy
VL  - 50
IS  - 3-4
SP  - 1013
EP  - 1018
DO  - 10.1016/j.fct.2011.12.030
ER  - 
@article{
author = "Grozdanović, Milica and Popović, Milica and Polović, Natalija and Burazer, Lidija M. and Vuckovic, Olga and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1286",
abstract = "Actinidin, an abundant cysteine protease from kiwifruit, is a specific biomarker of isolated allergy to kiwifruit. This study evaluates the IgE-binding properties of biologically active and thermally inactivated actinidin. Employing two different activity assays (caseinolytic assay and zymogram with gelatin) we showed that actinidin obtained from kiwifruit extract under native conditions represents a mixture of inactive and active enzyme. The structural integrity of actinidin was confirmed by SDS-PAGE. Edman degradation, mass fingerprint and Western blot with polyclonal antibodies. Although it was capable of inducing positive skin prick test reactions, we failed to detect IgE reactivity of active actinidin in Western blot with patient sera. Thermally inactivated actinidin exhibited IgE reactivity both in vivo and in vitro, indicating that heat processed kiwifruit products may induce clinical reactivity. These findings imply that apart from the allergenic epitopes on its surface, actinidin also contains hidden epitopes inside the protein which become accessible to IgE upon thermal treatment. (C) 2011 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Food and Chemical Toxicology",
title = "Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy",
volume = "50",
number = "3-4",
pages = "1013-1018",
doi = "10.1016/j.fct.2011.12.030"
}
Grozdanović, M., Popović, M., Polović, N., Burazer, L. M., Vuckovic, O., Atanasković-Marković, M., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M. (2012). Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy.
Food and Chemical Toxicology
Pergamon-Elsevier Science Ltd, Oxford., 50(3-4), 1013-1018.
https://doi.org/10.1016/j.fct.2011.12.030
Grozdanović M, Popović M, Polović N, Burazer LM, Vuckovic O, Atanasković-Marković M, Lindner B, Petersen A, Gavrović-Jankulović M. Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy. Food and Chemical Toxicology. 2012;50(3-4):1013-1018
Grozdanović Milica, Popović Milica, Polović Natalija, Burazer Lidija M., Vuckovic Olga, Atanasković-Marković Marina, Lindner Buko, Petersen Arnd, Gavrović-Jankulović Marija, "Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy" Food and Chemical Toxicology, 50, no. 3-4 (2012):1013-1018,
https://doi.org/10.1016/j.fct.2011.12.030 .
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