TY  - JOUR
AU  - Minić, Rajna
AU  - Josipović, Mirjana
AU  - Tomić Spirić, Vesna
AU  - Gavrović-Jankulović, Marija
AU  - Perić Popadić, Aleksandra
AU  - Prokopijević, Ivana
AU  - Ljubičić, Ana
AU  - Stamenković, Danijela
AU  - Burazer, Lidija M.
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3883
AB  - Background and objectives: The relationship between air pollen quantity and the sensitization of allergic patients is crucial for both the diagnosis and treatment of allergic diseases. Weather conditions influence the distribution of allergenic pollen and increases in pollen concentration may negatively affect the health of allergic patients. The aim of this study was to analyze the implementation of allergen immunotherapy with regard to air pollen concentration. Material and Methods: Here we examined the relationship between Betula air pollen concentration and the usage of Betula verrucosa allergen immunotherapy in Serbia. Examination covered the period from 2015 to 2018. Measurement of airborne pollen concentration was performed with Lanzoni volumetric pollen traps. The evidence of the usage of sublingual allergen immunotherapy (SLIT) was gathered from patients with documented sensitization to specific pollen. Results: During this period tree pollens were represented with 58% ± 21% of all measured air pollen species, while Betula pollen represented 15% ± 8% of all tree pollens. Betula pollination peaked in April. Allergen immunotherapy to Betula verrucosa in Serbia is entirely conducted as sublingual immunotherapy and represents 47.1% ± 1.4% of issued tree pollen SLIT. The use of pollen SLIT increased by 68% from 2015 to 2018, with an even greater increase in usage recorded for Betula SLIT—80%. Conclusions: This analysis shows a clear causative relationship between pollination and the type/prevalence of applied allergen immunotherapy. Information about the flowering seasons of allergenic plants is very important for people who suffer from allergy, for clinical allergologists, as well as for governing authorities. The presented data is of practical importance to the proper timing of immunotherapy initiation and of importance for urban landscaping. The obtained data can be the starting point for the instatement of a thorough epidemiological study and the inclusion of Serbia on the pollen map of Europe.
PB  - MDPI
T2  - Medicina (Lithuania)
T1  - Impact of tree pollen distribution on allergic diseases in serbia: Evidence of implementation of allergen immunotherapy to Betula verrucosa
VL  - 56
IS  - 2
DO  - 10.3390/medicina56020059
ER  - 

@article{
author = "Minić, Rajna and Josipović, Mirjana and Tomić Spirić, Vesna and Gavrović-Jankulović, Marija and Perić Popadić, Aleksandra and Prokopijević, Ivana and Ljubičić, Ana and Stamenković, Danijela and Burazer, Lidija M.",
year = "2020",
abstract = "Background and objectives: The relationship between air pollen quantity and the sensitization of allergic patients is crucial for both the diagnosis and treatment of allergic diseases. Weather conditions influence the distribution of allergenic pollen and increases in pollen concentration may negatively affect the health of allergic patients. The aim of this study was to analyze the implementation of allergen immunotherapy with regard to air pollen concentration. Material and Methods: Here we examined the relationship between Betula air pollen concentration and the usage of Betula verrucosa allergen immunotherapy in Serbia. Examination covered the period from 2015 to 2018. Measurement of airborne pollen concentration was performed with Lanzoni volumetric pollen traps. The evidence of the usage of sublingual allergen immunotherapy (SLIT) was gathered from patients with documented sensitization to specific pollen. Results: During this period tree pollens were represented with 58% ± 21% of all measured air pollen species, while Betula pollen represented 15% ± 8% of all tree pollens. Betula pollination peaked in April. Allergen immunotherapy to Betula verrucosa in Serbia is entirely conducted as sublingual immunotherapy and represents 47.1% ± 1.4% of issued tree pollen SLIT. The use of pollen SLIT increased by 68% from 2015 to 2018, with an even greater increase in usage recorded for Betula SLIT—80%. Conclusions: This analysis shows a clear causative relationship between pollination and the type/prevalence of applied allergen immunotherapy. Information about the flowering seasons of allergenic plants is very important for people who suffer from allergy, for clinical allergologists, as well as for governing authorities. The presented data is of practical importance to the proper timing of immunotherapy initiation and of importance for urban landscaping. The obtained data can be the starting point for the instatement of a thorough epidemiological study and the inclusion of Serbia on the pollen map of Europe.",
publisher = "MDPI",
journal = "Medicina (Lithuania)",
title = "Impact of tree pollen distribution on allergic diseases in serbia: Evidence of implementation of allergen immunotherapy to Betula verrucosa",
volume = "56",
number = "2",
doi = "10.3390/medicina56020059"
}

Minić, R., Josipović, M., Tomić Spirić, V., Gavrović-Jankulović, M., Perić Popadić, A., Prokopijević, I., Ljubičić, A., Stamenković, D.,& Burazer, L. M.. (2020). Impact of tree pollen distribution on allergic diseases in serbia: Evidence of implementation of allergen immunotherapy to Betula verrucosa. in Medicina (Lithuania)
MDPI., 56(2).
https://doi.org/10.3390/medicina56020059

Minić R, Josipović M, Tomić Spirić V, Gavrović-Jankulović M, Perić Popadić A, Prokopijević I, Ljubičić A, Stamenković D, Burazer LM. Impact of tree pollen distribution on allergic diseases in serbia: Evidence of implementation of allergen immunotherapy to Betula verrucosa. in Medicina (Lithuania). 2020;56(2).
doi:10.3390/medicina56020059 .

Minić, Rajna, Josipović, Mirjana, Tomić Spirić, Vesna, Gavrović-Jankulović, Marija, Perić Popadić, Aleksandra, Prokopijević, Ivana, Ljubičić, Ana, Stamenković, Danijela, Burazer, Lidija M., "Impact of tree pollen distribution on allergic diseases in serbia: Evidence of implementation of allergen immunotherapy to Betula verrucosa" in Medicina (Lithuania), 56, no. 2 (2020),
https://doi.org/10.3390/medicina56020059 . .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljković, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3737
PB  - Wiley
C3  - Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
T1  - In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress
VL  - 74
IS  - supp. 106
SP  - 878
EP  - 878
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3737
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljković, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
publisher = "Wiley",
journal = "Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)",
title = "In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress",
volume = "74",
number = "supp. 106",
pages = "878-878",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3737"
}

Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljković, Đ., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress. in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
Wiley., 74(supp. 106), 878-878.
https://hdl.handle.net/21.15107/rcub_cherry_3737

Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljković Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress. in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI). 2019;74(supp. 106):878-878.
https://hdl.handle.net/21.15107/rcub_cherry_3737 .

Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Cvetković, Anka, Veljković, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress" in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI), 74, no. supp. 106 (2019):878-878,
https://hdl.handle.net/21.15107/rcub_cherry_3737 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3742
AB  - Field-realistic exposure studies provide the most relevant assessment of the
effects of the intensity and diversity of urban and industrial contamination on
pollen structure and allergenicity. The significance of in-depth post-translational
modification (PTM) studies of pollen proteomes, when compared with studies on
other aspects of pollution and altered pollen allergenicity, has not yet been
determined; hence, little progress has been made within this field.
PB  - Belgrade : Faculty of Chemistry
C3  - 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
T1  - Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments
SP  - 6
EP  - 7
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3742
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Field-realistic exposure studies provide the most relevant assessment of the
effects of the intensity and diversity of urban and industrial contamination on
pollen structure and allergenicity. The significance of in-depth post-translational
modification (PTM) studies of pollen proteomes, when compared with studies on
other aspects of pollution and altered pollen allergenicity, has not yet been
determined; hence, little progress has been made within this field.",
publisher = "Belgrade : Faculty of Chemistry",
journal = "1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia",
title = "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments",
pages = "6-7",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3742"
}

Smiljanić, K., Prodić, I., Apostolović, D., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments. in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
Belgrade : Faculty of Chemistry., 6-7.
https://hdl.handle.net/21.15107/rcub_cherry_3742

Smiljanić K, Prodić I, Apostolović D, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments. in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia. 2019;:6-7.
https://hdl.handle.net/21.15107/rcub_cherry_3742 .

Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments" in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia (2019):6-7,
https://hdl.handle.net/21.15107/rcub_cherry_3742 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3763
AB  - The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. 
Therefore, we created a comprehensive approach for the comparison of pollen from polluted and environmentally preserved areas. To examine the effects of long-term, in vivo pollen exposure to multiple source pollutants, Phleum pratense (Timothy grass) pollen samples were collected along a regional road in Kruševac, central Serbia and were compared with pollen samples from rural, environmentally preserved area over two consecutive pollination seasons. We combined the quantitative comparison of proteome expression profiles from in-solution and 2D-gels with unrestrictive in-depth quantitative PTM profiling using high resolution tandem mass spectrometry and the PEAKS 8.5 Suite platform.
An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, and significantly higher content of mercury, cadmium, and manganese. Antioxidative defense-related enzymes were significantly upregulated. Seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected pollen allergens, especially Phl p 6, with several different oxidative modifications. 
Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach was used for the first time to map extensive modifications in the pollen proteome, reflecting increased environmental oxidative stress, primarily caused by increased content of heavy metals in pollen.
C3  - XIV Italian Proteomics Association Annual Meeting with HPS, 2019.
T1  - Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution
SP  - 38
EP  - 38
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3763
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. 
Therefore, we created a comprehensive approach for the comparison of pollen from polluted and environmentally preserved areas. To examine the effects of long-term, in vivo pollen exposure to multiple source pollutants, Phleum pratense (Timothy grass) pollen samples were collected along a regional road in Kruševac, central Serbia and were compared with pollen samples from rural, environmentally preserved area over two consecutive pollination seasons. We combined the quantitative comparison of proteome expression profiles from in-solution and 2D-gels with unrestrictive in-depth quantitative PTM profiling using high resolution tandem mass spectrometry and the PEAKS 8.5 Suite platform.
An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, and significantly higher content of mercury, cadmium, and manganese. Antioxidative defense-related enzymes were significantly upregulated. Seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected pollen allergens, especially Phl p 6, with several different oxidative modifications. 
Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach was used for the first time to map extensive modifications in the pollen proteome, reflecting increased environmental oxidative stress, primarily caused by increased content of heavy metals in pollen.",
journal = "XIV Italian Proteomics Association Annual Meeting with HPS, 2019.",
title = "Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution",
pages = "38-38",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3763"
}

Smiljanić, K., Prodić, I., Apostolović, D., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution. in XIV Italian Proteomics Association Annual Meeting with HPS, 2019., 38-38.
https://hdl.handle.net/21.15107/rcub_cherry_3763

Smiljanić K, Prodić I, Apostolović D, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution. in XIV Italian Proteomics Association Annual Meeting with HPS, 2019.. 2019;:38-38.
https://hdl.handle.net/21.15107/rcub_cherry_3763 .

Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution" in XIV Italian Proteomics Association Annual Meeting with HPS, 2019. (2019):38-38,
https://hdl.handle.net/21.15107/rcub_cherry_3763 .

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2857
AB  - An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.
PB  - Elsevier
T2  - Environment International
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress
VL  - 126
SP  - 644
EP  - 658
DO  - 10.1016/j.envint.2019.03.001
ER  - 

@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.",
publisher = "Elsevier",
journal = "Environment International",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress",
volume = "126",
pages = "644-658",
doi = "10.1016/j.envint.2019.03.001"
}

Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International
Elsevier., 126, 644-658.
https://doi.org/10.1016/j.envint.2019.03.001

Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljović Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International. 2019;126:644-658.
doi:10.1016/j.envint.2019.03.001 .

Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Cvetković, Anka, Veljović, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress" in Environment International, 126 (2019):644-658,
https://doi.org/10.1016/j.envint.2019.03.001 . .

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3224
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 

@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}

Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113

Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .

Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović-Vesić, Jelena, Radibratović, Milica, Radosavljević, Jelena, Burazer, Lidija M., Milčić, Miloš K., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2155
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 

@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}

Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113

Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .

Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović-Vesić, Jelena, Radibratović, Milica, Radosavljević, Jelena, Burazer, Lidija M., Milčić, Miloš K., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .

TY  - CONF
AU  - Radosavljević, Jelena
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2176
PB  - Wiley, Hoboken
C3  - FEBS OPEN BIO
T1  - Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes
VL  - 8
SP  - 257
EP  - 257
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2176
ER  - 

@conference{
author = "Radosavljević, Jelena and Apostolović, Danijela and Mihailović-Vesić, Jelena and Atanasković-Marković, Marina and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "FEBS OPEN BIO",
title = "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes",
volume = "8",
pages = "257-257",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2176"
}

Radosavljević, J., Apostolović, D., Mihailović-Vesić, J., Atanasković-Marković, M., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T.. (2018). Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes. in FEBS OPEN BIO
Wiley, Hoboken., 8, 257-257.
https://hdl.handle.net/21.15107/rcub_cherry_2176

Radosavljević J, Apostolović D, Mihailović-Vesić J, Atanasković-Marković M, Burazer LM, van Hage M, Ćirković-Veličković T. Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes. in FEBS OPEN BIO. 2018;8:257-257.
https://hdl.handle.net/21.15107/rcub_cherry_2176 .

Radosavljević, Jelena, Apostolović, Danijela, Mihailović-Vesić, Jelena, Atanasković-Marković, Marina, Burazer, Lidija M., van Hage, Marianne, Ćirković-Veličković, Tanja, "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes" in FEBS OPEN BIO, 8 (2018):257-257,
https://hdl.handle.net/21.15107/rcub_cherry_2176 .

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, Snežana S.
AU  - Ognjenović, J.
AU  - Peruško, Marija
AU  - Mihajlović, Luka
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2468
AB  - Background Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study
VL  - 47
IS  - 6
SP  - 815
EP  - 828
DO  - 10.1111/cea.12874
ER  - 

@article{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, Snežana S. and Ognjenović, J. and Peruško, Marija and Mihajlović, Luka and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Background Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study",
volume = "47",
number = "6",
pages = "815-828",
doi = "10.1111/cea.12874"
}

Smiljanić, K., Apostolović, D., Trifunović, S. S., Ognjenović, J., Peruško, M., Mihajlović, L., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T.. (2017). Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy
Wiley, Hoboken., 47(6), 815-828.
https://doi.org/10.1111/cea.12874

Smiljanić K, Apostolović D, Trifunović SS, Ognjenović J, Peruško M, Mihajlović L, Burazer LM, van Hage M, Ćirković-Veličković T. Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy. 2017;47(6):815-828.
doi:10.1111/cea.12874 .

Smiljanić, Katarina, Apostolović, Danijela, Trifunović, Snežana S., Ognjenović, J., Peruško, Marija, Mihajlović, Luka, Burazer, Lidija M., van Hage, Marianne, Ćirković-Veličković, Tanja, "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study" in Clinical and Experimental Allergy, 47, no. 6 (2017):815-828,
https://doi.org/10.1111/cea.12874 . .

TY  - DATA
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Mirkov, Ivana
AU  - Apostolović, Danijela
AU  - Burazer, Lidija M.
AU  - Atanasković-Marković, Marina
AU  - Kataranovski, Milena
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3528
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3528
ER  - 

@misc{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Mirkov, Ivana and Apostolović, Danijela and Burazer, Lidija M. and Atanasković-Marković, Marina and Kataranovski, Milena and Ćirković-Veličković, Tanja",
year = "2016",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3528"
}

Stanić-Vučinić, D., Stojadinović, M. M., Mirkov, I., Apostolović, D., Burazer, L. M., Atanasković-Marković, M., Kataranovski, M.,& Ćirković-Veličković, T.. (2016). Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j. in RSC Advances
Royal Soc Chemistry, Cambridge..
https://hdl.handle.net/21.15107/rcub_cherry_3528

Stanić-Vučinić D, Stojadinović MM, Mirkov I, Apostolović D, Burazer LM, Atanasković-Marković M, Kataranovski M, Ćirković-Veličković T. Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j. in RSC Advances. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3528 .

Stanić-Vučinić, Dragana, Stojadinović, Marija M., Mirkov, Ivana, Apostolović, Danijela, Burazer, Lidija M., Atanasković-Marković, Marina, Kataranovski, Milena, Ćirković-Veličković, Tanja, "Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j" in RSC Advances (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3528 .

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Mirkov, Ivana
AU  - Apostolović, Danijela
AU  - Burazer, Lidija M.
AU  - Atanasković-Marković, Marina
AU  - Kataranovski, Milena
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2321
AB  - Modified allergens are a safer and more efficient alternative to natural allergens for specific immunotherapy. As the modification of an allergen can diminish its immunogenicity due to the alteration of T-cell epitopes, in this paper we study the effects of a reversible chemical modification of Art v 1, the main allergen of mugwort pollen, on its allergenicity and immunogenicity. Modification of Art v 1 by cis-aconitylation into a polyanionic derivative (CAA) did not result in any significant structural alteration. However, IgE-binding epitopes on CAA were blocked, resulting in a reduced IgE-binding and basophil activation. Both proteins induced proliferation of CD3(+)CD4(+) T-cells in mugwort-allergic patients, but only unmodified allergens increased IL-4, IL-5 and IL-10 production. Rabbit and mouse anti-CAA antibodies exhibited cross-reactivity with native allergens and blocked human IgE-binding to Art v 1. Degradation of CAA by lysosomal fraction enzymes resulted in a similar set of peptides, harboring MHC class II-binding peptides, as unmodified proteins. Thus, cis-aconitylation modified Art v 1 had a significantly reduced allergenicity, whereas its immunogenicity was completely preserved. Acid-environment-responsive modification, which releases a full repertoire of native allergen epitopes within a particular site, can be considered a smart drug delivery system, which is able to deliver a therapeutically-effective dose in a controlled manner, and minimizes adverse side effects.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation
VL  - 6
IS  - 91
SP  - 88216
EP  - 88228
DO  - 10.1039/c6ra17261j
ER  - 

@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Mirkov, Ivana and Apostolović, Danijela and Burazer, Lidija M. and Atanasković-Marković, Marina and Kataranovski, Milena and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "Modified allergens are a safer and more efficient alternative to natural allergens for specific immunotherapy. As the modification of an allergen can diminish its immunogenicity due to the alteration of T-cell epitopes, in this paper we study the effects of a reversible chemical modification of Art v 1, the main allergen of mugwort pollen, on its allergenicity and immunogenicity. Modification of Art v 1 by cis-aconitylation into a polyanionic derivative (CAA) did not result in any significant structural alteration. However, IgE-binding epitopes on CAA were blocked, resulting in a reduced IgE-binding and basophil activation. Both proteins induced proliferation of CD3(+)CD4(+) T-cells in mugwort-allergic patients, but only unmodified allergens increased IL-4, IL-5 and IL-10 production. Rabbit and mouse anti-CAA antibodies exhibited cross-reactivity with native allergens and blocked human IgE-binding to Art v 1. Degradation of CAA by lysosomal fraction enzymes resulted in a similar set of peptides, harboring MHC class II-binding peptides, as unmodified proteins. Thus, cis-aconitylation modified Art v 1 had a significantly reduced allergenicity, whereas its immunogenicity was completely preserved. Acid-environment-responsive modification, which releases a full repertoire of native allergen epitopes within a particular site, can be considered a smart drug delivery system, which is able to deliver a therapeutically-effective dose in a controlled manner, and minimizes adverse side effects.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation",
volume = "6",
number = "91",
pages = "88216-88228",
doi = "10.1039/c6ra17261j"
}

Stanić-Vučinić, D., Stojadinović, M. M., Mirkov, I., Apostolović, D., Burazer, L. M., Atanasković-Marković, M., Kataranovski, M.,& Ćirković-Veličković, T.. (2016). Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation. in RSC Advances
Royal Soc Chemistry, Cambridge., 6(91), 88216-88228.
https://doi.org/10.1039/c6ra17261j

Stanić-Vučinić D, Stojadinović MM, Mirkov I, Apostolović D, Burazer LM, Atanasković-Marković M, Kataranovski M, Ćirković-Veličković T. Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation. in RSC Advances. 2016;6(91):88216-88228.
doi:10.1039/c6ra17261j .

Stanić-Vučinić, Dragana, Stojadinović, Marija M., Mirkov, Ivana, Apostolović, Danijela, Burazer, Lidija M., Atanasković-Marković, Marina, Kataranovski, Milena, Ćirković-Veličković, Tanja, "Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation" in RSC Advances, 6, no. 91 (2016):88216-88228,
https://doi.org/10.1039/c6ra17261j . .

TY  - JOUR
AU  - Mihajlovic, Luka
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1899
AB  - Phenolic composition of Ambrosia artemisiifolia L. pollen and sub-pollen particles (SPP) aqueous extracts was determined, using a novel extraction procedure. Total phenolic and flavonoid content was determined, as well as the antioxidative properties of the extract. Main components of water-soluble pollen phenolics are monoglycosides and malonyl-mono- and diglycosides of isorhamnetin, quercetin and kaempferol, while spermidine derivatives were identified as the dominant polyamides. SPP are similar in composition to pollen phenolics (predominant isorhamnetin and quercetin monoglycosides), but lacking small phenolic molecules ( lt 450 Da). Ethanol-based extraction protocol revealed one-third lower amount of total phenolics in SPP than in pollen. For the first time in any pollen species, SPP and pollen phenolic compositions were compared in detail, with an UHPLC/ESI-LTQ-Orbitrap-MS-MS approach, revealing the presence of spermidine derivatives in both SPP and pollen, not previously reported in Ambrosia species. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Phytochemistry
T1  - Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles
VL  - 109
SP  - 125
EP  - 132
DO  - 10.1016/j.phytochem.2014.10.022
ER  - 

@article{
author = "Mihajlovic, Luka and Radosavljević, Jelena and Burazer, Lidija M. and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2015",
abstract = "Phenolic composition of Ambrosia artemisiifolia L. pollen and sub-pollen particles (SPP) aqueous extracts was determined, using a novel extraction procedure. Total phenolic and flavonoid content was determined, as well as the antioxidative properties of the extract. Main components of water-soluble pollen phenolics are monoglycosides and malonyl-mono- and diglycosides of isorhamnetin, quercetin and kaempferol, while spermidine derivatives were identified as the dominant polyamides. SPP are similar in composition to pollen phenolics (predominant isorhamnetin and quercetin monoglycosides), but lacking small phenolic molecules ( lt 450 Da). Ethanol-based extraction protocol revealed one-third lower amount of total phenolics in SPP than in pollen. For the first time in any pollen species, SPP and pollen phenolic compositions were compared in detail, with an UHPLC/ESI-LTQ-Orbitrap-MS-MS approach, revealing the presence of spermidine derivatives in both SPP and pollen, not previously reported in Ambrosia species. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Phytochemistry",
title = "Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles",
volume = "109",
pages = "125-132",
doi = "10.1016/j.phytochem.2014.10.022"
}

Mihajlovic, L., Radosavljević, J., Burazer, L. M., Smiljanić, K.,& Ćirković-Veličković, T.. (2015). Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles. in Phytochemistry
Pergamon-Elsevier Science Ltd, Oxford., 109, 125-132.
https://doi.org/10.1016/j.phytochem.2014.10.022

Mihajlovic L, Radosavljević J, Burazer LM, Smiljanić K, Ćirković-Veličković T. Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles. in Phytochemistry. 2015;109:125-132.
doi:10.1016/j.phytochem.2014.10.022 .

Mihajlovic, Luka, Radosavljević, Jelena, Burazer, Lidija M., Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles" in Phytochemistry, 109 (2015):125-132,
https://doi.org/10.1016/j.phytochem.2014.10.022 . .

TY  - JOUR
AU  - Aleksić, Ivana
AU  - Vučković, Olga
AU  - Smiljanić, Katarina
AU  - Gavrović-Jankulović, Marija
AU  - Krsmanovic, Vera
AU  - Burazer, Lidija M.
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1478
AB  - According to the data obtained from in vivo and in vitro testing in Serbia, a significant number of patients have allergic symptoms caused by grass pollen. We examined the protein composition of grass pollens (Dactylis glomerata, Lolium perenne and Phleum pratense) and cross-reactivity in patients allergic to grass pollen from our region. The grass pollen allergen extract was characterized by SDS-PAGE, while cross-reactivity of single grass pollens was revealed by immunoblot analysis. A high degree of cross-reactivity was demonstrated for all three single pollens in the sera of allergic patients compared to the grass pollen extract mixture. Confirmation of the existence of cross-reactivity between different antigenic sources facilitates the use of monovalent vaccines, which are easier to standardize and at the same time prevent further sensitization of patients and reduces adverse reactions.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of biological sciences
T1  - The Importance of Cross-Reactivity in Grass Pollen Allergy
VL  - 66
IS  - 3
SP  - 1149
EP  - 1155
DO  - 10.2298/ABS1403149A
ER  - 

@article{
author = "Aleksić, Ivana and Vučković, Olga and Smiljanić, Katarina and Gavrović-Jankulović, Marija and Krsmanovic, Vera and Burazer, Lidija M.",
year = "2014",
abstract = "According to the data obtained from in vivo and in vitro testing in Serbia, a significant number of patients have allergic symptoms caused by grass pollen. We examined the protein composition of grass pollens (Dactylis glomerata, Lolium perenne and Phleum pratense) and cross-reactivity in patients allergic to grass pollen from our region. The grass pollen allergen extract was characterized by SDS-PAGE, while cross-reactivity of single grass pollens was revealed by immunoblot analysis. A high degree of cross-reactivity was demonstrated for all three single pollens in the sera of allergic patients compared to the grass pollen extract mixture. Confirmation of the existence of cross-reactivity between different antigenic sources facilitates the use of monovalent vaccines, which are easier to standardize and at the same time prevent further sensitization of patients and reduces adverse reactions.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of biological sciences",
title = "The Importance of Cross-Reactivity in Grass Pollen Allergy",
volume = "66",
number = "3",
pages = "1149-1155",
doi = "10.2298/ABS1403149A"
}

Aleksić, I., Vučković, O., Smiljanić, K., Gavrović-Jankulović, M., Krsmanovic, V.,& Burazer, L. M.. (2014). The Importance of Cross-Reactivity in Grass Pollen Allergy. in Archives of biological sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 66(3), 1149-1155.
https://doi.org/10.2298/ABS1403149A

Aleksić I, Vučković O, Smiljanić K, Gavrović-Jankulović M, Krsmanovic V, Burazer LM. The Importance of Cross-Reactivity in Grass Pollen Allergy. in Archives of biological sciences. 2014;66(3):1149-1155.
doi:10.2298/ABS1403149A .

Aleksić, Ivana, Vučković, Olga, Smiljanić, Katarina, Gavrović-Jankulović, Marija, Krsmanovic, Vera, Burazer, Lidija M., "The Importance of Cross-Reactivity in Grass Pollen Allergy" in Archives of biological sciences, 66, no. 3 (2014):1149-1155,
https://doi.org/10.2298/ABS1403149A . .

TY  - JOUR
AU  - Popović, Milica M.
AU  - Anđelković, Uroš
AU  - Burazer, Lidija M.
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://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 M. and Anđelković, Uroš and Burazer, Lidija M. and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2013",
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. 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). in Phytochemistry
Pergamon-Elsevier Science Ltd, Oxford., 94, 53-59.
https://doi.org/10.1016/j.phytochem.2013.06.006

Popović MM, 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). in Phytochemistry. 2013;94:53-59.
doi:10.1016/j.phytochem.2013.06.006 .

Popović, Milica M., 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)" in Phytochemistry, 94 (2013):53-59,
https://doi.org/10.1016/j.phytochem.2013.06.006 . .

TY  - CONF
AU  - Burazer, Lidija M.
AU  - Aleksic, I
AU  - Vučković, O.
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1411
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Importance of sIgE measurement in evaluation of Dermatophagoides pteronyssinus major allergens in pediatric population
VL  - 68
SP  - 689
EP  - 689
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1411
ER  - 

@conference{
author = "Burazer, Lidija M. and Aleksic, I and Vučković, O. and Gavrović-Jankulović, Marija",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Importance of sIgE measurement in evaluation of Dermatophagoides pteronyssinus major allergens in pediatric population",
volume = "68",
pages = "689-689",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1411"
}

Burazer, L. M., Aleksic, I., Vučković, O.,& Gavrović-Jankulović, M.. (2013). Importance of sIgE measurement in evaluation of Dermatophagoides pteronyssinus major allergens in pediatric population. in Allergy
Wiley-Blackwell, Hoboken., 68, 689-689.
https://hdl.handle.net/21.15107/rcub_cherry_1411

Burazer LM, Aleksic I, Vučković O, Gavrović-Jankulović M. Importance of sIgE measurement in evaluation of Dermatophagoides pteronyssinus major allergens in pediatric population. in Allergy. 2013;68:689-689.
https://hdl.handle.net/21.15107/rcub_cherry_1411 .

Burazer, Lidija M., Aleksic, I, Vučković, O., Gavrović-Jankulović, Marija, "Importance of sIgE measurement in evaluation of Dermatophagoides pteronyssinus major allergens in pediatric population" in Allergy, 68 (2013):689-689,
https://hdl.handle.net/21.15107/rcub_cherry_1411 .

TY  - JOUR
AU  - Ognjenović, Jana
AU  - Milčić-Matić, Natalija
AU  - Smiljanić, Katarina
AU  - Vučković, Olga
AU  - Burazer, Lidija M.
AU  - Popović, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1391
AB  - Canine atopic dermatitis (CAD) is an immune system disorder that affects 10-15% of the canine population. Short ragweed (Ambrosia artemisiifolia) pollen represents one of the major seasonal sources of allergenic pollen proteins in Europe, particularly in the Pannonian valley of the Balkan region. In Serbia, about 66% of atopic dogs showed a positive intradermal skin test with its pollen extract, which is second to house dust mites. Therefore, characterization of Ambrosia artemisiifolia pollen components, in terms of defining major and minor allergens that induce clinically manifested allergic reaction in dogs, is important for valid diagnosis and efficient therapy. This study has, for the first time, characterized and identified major Ambrosia artemisiifolia allergens in CAD, using an immunoproteomic approach. To assess the prevalence of specific IgE in electrophoretically separated ragweed pollen proteins, individual reactivity of sera from dogs with CAD was analyzed and compared to the reactivity of sera from healthy dogs in the non-reducing conditions, which were found optimal for specific canine IgE detection. A specific IgE band (38 kDa) was recognized as the most dominant allergen in CAD, occurring in 81% of positive dog's sera. 2-D immunoblotting followed by a mass spectrometry peptide fingerprint analyses with pooled canine and human atopic sera, revealed that 38 kDa major Ambrosia atremisiifolia allergens in CAD were all five isoallergens of the Amb a 1 group (antigen E), including the previously named Amb a 2 (antigen K). In contrast to canine sera, human atopic sera also recognized lower mass allergens such as the 13 fragment of Amb a 1 and profilins (Amb a 8 variants). The most prominent ragweed proteins in CAD, represent, as in humans, variants of all five isoallergens of the Amb a 1 group (pectate lyase): Amb a 1.0101 and its natural variant E1XUL2, Amb a 1.0202, 1.0304, 1.0402 and the natural variant of Amb a 1.0501, E1XUM0, as well as the a fragment of pollen allergen Amb a 1.0201.
PB  - Elsevier Science Bv, Amsterdam
T2  - Veterinary Immunology and Immunopathology
T1  - Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis
VL  - 155
IS  - 1-2
SP  - 38
EP  - 47
DO  - 10.1016/j.vetimm.2013.06.005
ER  - 

@article{
author = "Ognjenović, Jana and Milčić-Matić, Natalija and Smiljanić, Katarina and Vučković, Olga and Burazer, Lidija M. and Popović, Nikola and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2013",
abstract = "Canine atopic dermatitis (CAD) is an immune system disorder that affects 10-15% of the canine population. Short ragweed (Ambrosia artemisiifolia) pollen represents one of the major seasonal sources of allergenic pollen proteins in Europe, particularly in the Pannonian valley of the Balkan region. In Serbia, about 66% of atopic dogs showed a positive intradermal skin test with its pollen extract, which is second to house dust mites. Therefore, characterization of Ambrosia artemisiifolia pollen components, in terms of defining major and minor allergens that induce clinically manifested allergic reaction in dogs, is important for valid diagnosis and efficient therapy. This study has, for the first time, characterized and identified major Ambrosia artemisiifolia allergens in CAD, using an immunoproteomic approach. To assess the prevalence of specific IgE in electrophoretically separated ragweed pollen proteins, individual reactivity of sera from dogs with CAD was analyzed and compared to the reactivity of sera from healthy dogs in the non-reducing conditions, which were found optimal for specific canine IgE detection. A specific IgE band (38 kDa) was recognized as the most dominant allergen in CAD, occurring in 81% of positive dog's sera. 2-D immunoblotting followed by a mass spectrometry peptide fingerprint analyses with pooled canine and human atopic sera, revealed that 38 kDa major Ambrosia atremisiifolia allergens in CAD were all five isoallergens of the Amb a 1 group (antigen E), including the previously named Amb a 2 (antigen K). In contrast to canine sera, human atopic sera also recognized lower mass allergens such as the 13 fragment of Amb a 1 and profilins (Amb a 8 variants). The most prominent ragweed proteins in CAD, represent, as in humans, variants of all five isoallergens of the Amb a 1 group (pectate lyase): Amb a 1.0101 and its natural variant E1XUL2, Amb a 1.0202, 1.0304, 1.0402 and the natural variant of Amb a 1.0501, E1XUM0, as well as the a fragment of pollen allergen Amb a 1.0201.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Veterinary Immunology and Immunopathology",
title = "Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis",
volume = "155",
number = "1-2",
pages = "38-47",
doi = "10.1016/j.vetimm.2013.06.005"
}

Ognjenović, J., Milčić-Matić, N., Smiljanić, K., Vučković, O., Burazer, L. M., Popović, N., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2013). Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis. in Veterinary Immunology and Immunopathology
Elsevier Science Bv, Amsterdam., 155(1-2), 38-47.
https://doi.org/10.1016/j.vetimm.2013.06.005

Ognjenović J, Milčić-Matić N, Smiljanić K, Vučković O, Burazer LM, Popović N, Stanić-Vučinić D, Ćirković-Veličković T. Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis. in Veterinary Immunology and Immunopathology. 2013;155(1-2):38-47.
doi:10.1016/j.vetimm.2013.06.005 .

Ognjenović, Jana, Milčić-Matić, Natalija, Smiljanić, Katarina, Vučković, Olga, Burazer, Lidija M., Popović, Nikola, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis" in Veterinary Immunology and Immunopathology, 155, no. 1-2 (2013):38-47,
https://doi.org/10.1016/j.vetimm.2013.06.005 . .

TY  - DATA
AU  - Grozdanović, Milica M.
AU  - Burazer, Lidija M.
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3502
PB  - Elsevier Sci Ltd, Oxford
T2  - International Dairy Journal
T1  - Supplementary data for article: Grozdanović, M. M.; Burazer, L. M.; Gavrović-Jankulović, M. Kiwifruit (Actinidia Deliciosa) Extract Shows Potential as a Low-Cost and Efficient Milk-Clotting Agent. International Dairy Journal 2013, 32 (1), 46–52. https://doi.org/10.1016/j.idairyj.2013.03.001
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3502
ER  - 

@misc{
author = "Grozdanović, Milica M. and Burazer, Lidija M. and Gavrović-Jankulović, Marija",
year = "2013",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Dairy Journal",
title = "Supplementary data for article: Grozdanović, M. M.; Burazer, L. M.; Gavrović-Jankulović, M. Kiwifruit (Actinidia Deliciosa) Extract Shows Potential as a Low-Cost and Efficient Milk-Clotting Agent. International Dairy Journal 2013, 32 (1), 46–52. https://doi.org/10.1016/j.idairyj.2013.03.001",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3502"
}

Grozdanović, M. M., Burazer, L. M.,& Gavrović-Jankulović, M.. (2013). Supplementary data for article: Grozdanović, M. M.; Burazer, L. M.; Gavrović-Jankulović, M. Kiwifruit (Actinidia Deliciosa) Extract Shows Potential as a Low-Cost and Efficient Milk-Clotting Agent. International Dairy Journal 2013, 32 (1), 46–52. https://doi.org/10.1016/j.idairyj.2013.03.001. in International Dairy Journal
Elsevier Sci Ltd, Oxford..
https://hdl.handle.net/21.15107/rcub_cherry_3502

Grozdanović MM, Burazer LM, Gavrović-Jankulović M. Supplementary data for article: Grozdanović, M. M.; Burazer, L. M.; Gavrović-Jankulović, M. Kiwifruit (Actinidia Deliciosa) Extract Shows Potential as a Low-Cost and Efficient Milk-Clotting Agent. International Dairy Journal 2013, 32 (1), 46–52. https://doi.org/10.1016/j.idairyj.2013.03.001. in International Dairy Journal. 2013;.
https://hdl.handle.net/21.15107/rcub_cherry_3502 .

Grozdanović, Milica M., Burazer, Lidija M., Gavrović-Jankulović, Marija, "Supplementary data for article: Grozdanović, M. M.; Burazer, L. M.; Gavrović-Jankulović, M. Kiwifruit (Actinidia Deliciosa) Extract Shows Potential as a Low-Cost and Efficient Milk-Clotting Agent. International Dairy Journal 2013, 32 (1), 46–52. https://doi.org/10.1016/j.idairyj.2013.03.001" in International Dairy Journal (2013),
https://hdl.handle.net/21.15107/rcub_cherry_3502 .

TY  - JOUR
AU  - Milčić-Matić, Natalija
AU  - Ognjenović, Jana
AU  - Burazer, Lidija M.
AU  - Blagojević, G.
AU  - Popović, Nikola
AU  - Lazarevic, M.
AU  - Stanić-Vučinić, Dragana
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1407
AB  - Common ragweed (Ambrosia atremisiifolia) is one of the most frequent causes of pollen-induced allergic reactions both in humans and dogs. It has not been defined yet, what is the major allergen(s) to which most dogs allergic to ragweed show a positive result on intradermal skin test (IDST). In the present study sensitization to Ambrosia artemisiifolia pollen allergens in dogs with atopic dermatitis was examined with both in vivo and in vitro tests, including IDST and serum allergen specific IgE test. Detection of specific-IgE antibodies against ragweed allergens by immunoblotting in the sera of allergic dogs was optimized, as well. Dogs that were positive, as judged by IDST reactions to ragweed pollen allergens, also had alergen specific IgE antibodies in their sera. Results indicate that major allergens of A. artemisifolia pollen in dogs are Amb a 1 and Amb a 2. Further characterization of ragweed allergens is needed before they could potentially be used in intradermal testing or allergen immunotherapy in affected dogs. Also, we evaluated new Favrots diagnostic criteria for canine atopic dermatitis in dogs allergic to Ambrosia atremisiifolia pollen. It might be concluded that proposed criteria are of great assistance for seting up suspected diagnosis of canine atopic dermatitis, after ruling out other pruritic dermatoses.
AB  - Kratka ambrozija (Ambrosia artemisiifolia) je jedan od najčešćih uzročnika alergijskih reakcija izazvanih polenom kod ljudi i pasa. Još uvek nije definisano koji je glavni alergen (i), na koji, većina pasa alergičnih na polen ambrozije, ispoljava pozitivnu reakciju na intradermalnom testu. U ovoj studiji je ispitana senzibilizacija na polen ove biljke kod pasa sa simptomima atopijskog dermatitisa in vivo i in vitro testovima, uključujući intradermalni test i dokazivanje prisustva alergen specifičnih IgE antitela u serumu. Optimizovani su uslovi za detekciju IgE specifičnih antitela iz seruma pasa alergičnih na polen ambrozije imunoblot tehnikom. Psi koji su imali pozitivnu reakciju na polen ove biljke na intradermalnom testu, takođe su imali specifična IgE antitela u serumu. Dobijeni rezultati ukazuju da su glavni alergeni Ambrosia artemisiifolia kod pasa Amb a 1 i Amb a 2. Neophodna je dalja karakterizacija alergena ambrozije kako bi se oni mogli primeniti pri rutinskom intradermalnom testiranju ili u alergen specifičnoj imunoterapiji obolelih pasa. Takođe je razmatrana i validnost Favrotovih dijagnostičkih kriterijuma kod pasa alergičnih na polen ambrozije. Može se zaključiti da su predloženi kriterijumi od velike pomoći u postavljanju suspektne dijagnoze atopijskog dermatitisa pasa, nakon isključenja drugih pruritičnih dermatoza.
PB  - De Gruyter Poland Sp Zoo, Warsaw
T2  - Acta Veterinaria, Beograd
T1  - Evaluation of Criteria for Diagnosis of Atopic Dermatitis and Detection of Allergen Specific Ige Antibodies in Dogs Allergic to Ambrosia Artemisiifolia Pollen
T1  - Evaluacija kriterijuma za dijagnozu atopijskog dermatitisa i detekcija alergen specifičnih IgE antitela kod pasa alergičnih na polen biljke Ambrosia artemisiifolia
VL  - 63
IS  - 4
SP  - 437
EP  - 451
DO  - 10.2298/AVB1304437M
ER  - 

@article{
author = "Milčić-Matić, Natalija and Ognjenović, Jana and Burazer, Lidija M. and Blagojević, G. and Popović, Nikola and Lazarevic, M. and Stanić-Vučinić, Dragana",
year = "2013",
abstract = "Common ragweed (Ambrosia atremisiifolia) is one of the most frequent causes of pollen-induced allergic reactions both in humans and dogs. It has not been defined yet, what is the major allergen(s) to which most dogs allergic to ragweed show a positive result on intradermal skin test (IDST). In the present study sensitization to Ambrosia artemisiifolia pollen allergens in dogs with atopic dermatitis was examined with both in vivo and in vitro tests, including IDST and serum allergen specific IgE test. Detection of specific-IgE antibodies against ragweed allergens by immunoblotting in the sera of allergic dogs was optimized, as well. Dogs that were positive, as judged by IDST reactions to ragweed pollen allergens, also had alergen specific IgE antibodies in their sera. Results indicate that major allergens of A. artemisifolia pollen in dogs are Amb a 1 and Amb a 2. Further characterization of ragweed allergens is needed before they could potentially be used in intradermal testing or allergen immunotherapy in affected dogs. Also, we evaluated new Favrots diagnostic criteria for canine atopic dermatitis in dogs allergic to Ambrosia atremisiifolia pollen. It might be concluded that proposed criteria are of great assistance for seting up suspected diagnosis of canine atopic dermatitis, after ruling out other pruritic dermatoses., Kratka ambrozija (Ambrosia artemisiifolia) je jedan od najčešćih uzročnika alergijskih reakcija izazvanih polenom kod ljudi i pasa. Još uvek nije definisano koji je glavni alergen (i), na koji, većina pasa alergičnih na polen ambrozije, ispoljava pozitivnu reakciju na intradermalnom testu. U ovoj studiji je ispitana senzibilizacija na polen ove biljke kod pasa sa simptomima atopijskog dermatitisa in vivo i in vitro testovima, uključujući intradermalni test i dokazivanje prisustva alergen specifičnih IgE antitela u serumu. Optimizovani su uslovi za detekciju IgE specifičnih antitela iz seruma pasa alergičnih na polen ambrozije imunoblot tehnikom. Psi koji su imali pozitivnu reakciju na polen ove biljke na intradermalnom testu, takođe su imali specifična IgE antitela u serumu. Dobijeni rezultati ukazuju da su glavni alergeni Ambrosia artemisiifolia kod pasa Amb a 1 i Amb a 2. Neophodna je dalja karakterizacija alergena ambrozije kako bi se oni mogli primeniti pri rutinskom intradermalnom testiranju ili u alergen specifičnoj imunoterapiji obolelih pasa. Takođe je razmatrana i validnost Favrotovih dijagnostičkih kriterijuma kod pasa alergičnih na polen ambrozije. Može se zaključiti da su predloženi kriterijumi od velike pomoći u postavljanju suspektne dijagnoze atopijskog dermatitisa pasa, nakon isključenja drugih pruritičnih dermatoza.",
publisher = "De Gruyter Poland Sp Zoo, Warsaw",
journal = "Acta Veterinaria, Beograd",
title = "Evaluation of Criteria for Diagnosis of Atopic Dermatitis and Detection of Allergen Specific Ige Antibodies in Dogs Allergic to Ambrosia Artemisiifolia Pollen, Evaluacija kriterijuma za dijagnozu atopijskog dermatitisa i detekcija alergen specifičnih IgE antitela kod pasa alergičnih na polen biljke Ambrosia artemisiifolia",
volume = "63",
number = "4",
pages = "437-451",
doi = "10.2298/AVB1304437M"
}

Milčić-Matić, N., Ognjenović, J., Burazer, L. M., Blagojević, G., Popović, N., Lazarevic, M.,& Stanić-Vučinić, D.. (2013). Evaluation of Criteria for Diagnosis of Atopic Dermatitis and Detection of Allergen Specific Ige Antibodies in Dogs Allergic to Ambrosia Artemisiifolia Pollen. in Acta Veterinaria, Beograd
De Gruyter Poland Sp Zoo, Warsaw., 63(4), 437-451.
https://doi.org/10.2298/AVB1304437M

Milčić-Matić N, Ognjenović J, Burazer LM, Blagojević G, Popović N, Lazarevic M, Stanić-Vučinić D. Evaluation of Criteria for Diagnosis of Atopic Dermatitis and Detection of Allergen Specific Ige Antibodies in Dogs Allergic to Ambrosia Artemisiifolia Pollen. in Acta Veterinaria, Beograd. 2013;63(4):437-451.
doi:10.2298/AVB1304437M .

Milčić-Matić, Natalija, Ognjenović, Jana, Burazer, Lidija M., Blagojević, G., Popović, Nikola, Lazarevic, M., Stanić-Vučinić, Dragana, "Evaluation of Criteria for Diagnosis of Atopic Dermatitis and Detection of Allergen Specific Ige Antibodies in Dogs Allergic to Ambrosia Artemisiifolia Pollen" in Acta Veterinaria, Beograd, 63, no. 4 (2013):437-451,
https://doi.org/10.2298/AVB1304437M . .

TY  - JOUR
AU  - Grozdanović, Milica M.
AU  - Burazer, Lidija M.
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1589
AB  - Actinidin, a cysteine protease accounting for more than 50% of the soluble proteins in kiwifruit pulp, has shown promise as a milk-clotting agent. In this study, the potential use of kiwifruit pulp extract as a clotting agent was investigated. It was shown that three kiwifruit extracts made from the pulp of a single fruit have significantly different levels of active actinidin, depending on the extraction buffer employed. Kiwifruit extract prepared at pH 5.0 had the best milk-clotting properties, with a nearly 30% better ratio of clotting activity to proteolytic activity than purified actinidin. This extract produced a casein coagulum clearly separated from the whey proteins, and was shown to be stable at room temperature for up to two months. This extract has the potential to be employed as an efficient and low-cost milk-clotting agent in the production of dairy products.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Dairy Journal
T1  - Kiwifruit (Actinidia deliciosa) extract shows potential as a low-cost and efficient milk-clotting agent
VL  - 32
IS  - 1
SP  - 46
EP  - 52
DO  - 10.1016/j.idairyj.2013.03.001
ER  - 

@article{
author = "Grozdanović, Milica M. and Burazer, Lidija M. and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "Actinidin, a cysteine protease accounting for more than 50% of the soluble proteins in kiwifruit pulp, has shown promise as a milk-clotting agent. In this study, the potential use of kiwifruit pulp extract as a clotting agent was investigated. It was shown that three kiwifruit extracts made from the pulp of a single fruit have significantly different levels of active actinidin, depending on the extraction buffer employed. Kiwifruit extract prepared at pH 5.0 had the best milk-clotting properties, with a nearly 30% better ratio of clotting activity to proteolytic activity than purified actinidin. This extract produced a casein coagulum clearly separated from the whey proteins, and was shown to be stable at room temperature for up to two months. This extract has the potential to be employed as an efficient and low-cost milk-clotting agent in the production of dairy products.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Dairy Journal",
title = "Kiwifruit (Actinidia deliciosa) extract shows potential as a low-cost and efficient milk-clotting agent",
volume = "32",
number = "1",
pages = "46-52",
doi = "10.1016/j.idairyj.2013.03.001"
}

Grozdanović, M. M., Burazer, L. M.,& Gavrović-Jankulović, M.. (2013). Kiwifruit (Actinidia deliciosa) extract shows potential as a low-cost and efficient milk-clotting agent. in International Dairy Journal
Elsevier Sci Ltd, Oxford., 32(1), 46-52.
https://doi.org/10.1016/j.idairyj.2013.03.001

Grozdanović MM, Burazer LM, Gavrović-Jankulović M. Kiwifruit (Actinidia deliciosa) extract shows potential as a low-cost and efficient milk-clotting agent. in International Dairy Journal. 2013;32(1):46-52.
doi:10.1016/j.idairyj.2013.03.001 .

Grozdanović, Milica M., Burazer, Lidija M., Gavrović-Jankulović, Marija, "Kiwifruit (Actinidia deliciosa) extract shows potential as a low-cost and efficient milk-clotting agent" in International Dairy Journal, 32, no. 1 (2013):46-52,
https://doi.org/10.1016/j.idairyj.2013.03.001 . .

TY  - CONF
AU  - Ognjenović, J.
AU  - Mihajlovic, L.
AU  - Stanić-Vučinić, Dragana
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1544
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals
VL  - 67
SP  - 638
EP  - 639
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1544
ER  - 

@conference{
author = "Ognjenović, J. and Mihajlovic, L. and Stanić-Vučinić, Dragana and Atanasković-Marković, Marina and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2012",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals",
volume = "67",
pages = "638-639",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1544"
}

Ognjenović, J., Mihajlovic, L., Stanić-Vučinić, D., Atanasković-Marković, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2012). Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals. in Allergy
Wiley-Blackwell, Hoboken., 67, 638-639.
https://hdl.handle.net/21.15107/rcub_cherry_1544

Ognjenović J, Mihajlovic L, Stanić-Vučinić D, Atanasković-Marković M, Burazer LM, Ćirković-Veličković T. Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals. in Allergy. 2012;67:638-639.
https://hdl.handle.net/21.15107/rcub_cherry_1544 .

Ognjenović, J., Mihajlovic, L., Stanić-Vučinić, Dragana, Atanasković-Marković, Marina, Burazer, Lidija M., Ćirković-Veličković, Tanja, "Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals" in Allergy, 67 (2012):638-639,
https://hdl.handle.net/21.15107/rcub_cherry_1544 .

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Burazer, Lidija M.
AU  - Ercili-Cura, Dilek
AU  - Sancho, Ana
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1275
AB  - BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry
PB  - Wiley-Blackwell, Malden
T2  - Journal of the Science of Food and Agriculture
T1  - One-step method for isolation and purification of native beta-lactoglobulin from bovine whey
VL  - 92
IS  - 7
SP  - 1432
EP  - 1440
DO  - 10.1002/jsfa.4722
ER  - 

@article{
author = "Stojadinović, Marija M. and Burazer, Lidija M. and Ercili-Cura, Dilek and Sancho, Ana and Buchert, Johanna and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2012",
abstract = "BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Malden",
journal = "Journal of the Science of Food and Agriculture",
title = "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey",
volume = "92",
number = "7",
pages = "1432-1440",
doi = "10.1002/jsfa.4722"
}

Stojadinović, M. M., Burazer, L. M., Ercili-Cura, D., Sancho, A., Buchert, J., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2012). One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Malden., 92(7), 1432-1440.
https://doi.org/10.1002/jsfa.4722

Stojadinović MM, Burazer LM, Ercili-Cura D, Sancho A, Buchert J, Ćirković-Veličković T, Stanić-Vučinić D. One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture. 2012;92(7):1432-1440.
doi:10.1002/jsfa.4722 .

Stojadinović, Marija M., Burazer, Lidija M., Ercili-Cura, Dilek, Sancho, Ana, Buchert, Johanna, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey" in Journal of the Science of Food and Agriculture, 92, no. 7 (2012):1432-1440,
https://doi.org/10.1002/jsfa.4722 . .

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica M.
AU  - Dimitrijevic, Rajna
AU  - Burazer, Lidija M.
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://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 M. and Dimitrijevic, Rajna and Burazer, Lidija M. and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
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. 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. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 77(1), 43-52.
https://doi.org/10.2298/JSC110309158A

Abughren M, Popović MM, Dimitrijevic R, Burazer LM, Grozdanović M, Atanasković-Marković M, Gavrović-Jankulović M. Optimization of the heterologous expression of banana glucanase in Escherichia coli. in Journal of the Serbian Chemical Society. 2012;77(1):43-52.
doi:10.2298/JSC110309158A .

Abughren, Mohamed, Popović, Milica M., Dimitrijevic, Rajna, Burazer, Lidija M., Grozdanović, Milica, Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, "Optimization of the heterologous expression of banana glucanase in Escherichia coli" in Journal of the Serbian Chemical Society, 77, no. 1 (2012):43-52,
https://doi.org/10.2298/JSC110309158A . .

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica M.
AU  - Dimitrijevic, Rajna
AU  - Burazer, Lidija M.
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://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
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1259
ER  - 

@article{
author = "Abughren, Mohamed and Popović, Milica M. and Dimitrijevic, Rajna and Burazer, Lidija M. and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
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",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1259"
}

Abughren, M., Popović, M. 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). in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 77(2), 257-258.
https://hdl.handle.net/21.15107/rcub_cherry_1259

Abughren M, Popović MM, 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). in Journal of the Serbian Chemical Society. 2012;77(2):257-258.
https://hdl.handle.net/21.15107/rcub_cherry_1259 .

Abughren, Mohamed, Popović, Milica M., 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)" in Journal of the Serbian Chemical Society, 77, no. 2 (2012):257-258,
https://hdl.handle.net/21.15107/rcub_cherry_1259 .

TY  - JOUR
AU  - Grozdanović, Milica
AU  - Popović, Milica M.
AU  - Polović, Natalija
AU  - Burazer, Lidija M.
AU  - Vučković, Olga
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://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 M. and Polović, Natalija and Burazer, Lidija M. and Vučković, Olga and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2012",
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. M., Polović, N., Burazer, L. M., Vučković, 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. in 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 MM, Polović N, Burazer LM, Vučković 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. in Food and Chemical Toxicology. 2012;50(3-4):1013-1018.
doi:10.1016/j.fct.2011.12.030 .

Grozdanović, Milica, Popović, Milica M., Polović, Natalija, Burazer, Lidija M., Vučković, 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" in Food and Chemical Toxicology, 50, no. 3-4 (2012):1013-1018,
https://doi.org/10.1016/j.fct.2011.12.030 . .

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Burazer, Lidija M.
AU  - Ercili-Cura, D.
AU  - Sancho, A.
AU  - Buchert, Johanna
AU  - Mills, C.
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1473
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms
VL  - 66
SP  - 523
EP  - 524
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1473
ER  - 

@conference{
author = "Stojadinović, Marija M. and Burazer, Lidija M. and Ercili-Cura, D. and Sancho, A. and Buchert, Johanna and Mills, C. and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2011",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms",
volume = "66",
pages = "523-524",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1473"
}

Stojadinović, M. M., Burazer, L. M., Ercili-Cura, D., Sancho, A., Buchert, J., Mills, C., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2011). An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms. in Allergy
Wiley-Blackwell, Hoboken., 66, 523-524.
https://hdl.handle.net/21.15107/rcub_cherry_1473

Stojadinović MM, Burazer LM, Ercili-Cura D, Sancho A, Buchert J, Mills C, Ćirković-Veličković T, Stanić-Vučinić D. An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms. in Allergy. 2011;66:523-524.
https://hdl.handle.net/21.15107/rcub_cherry_1473 .

Stojadinović, Marija M., Burazer, Lidija M., Ercili-Cura, D., Sancho, A., Buchert, Johanna, Mills, C., Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms" in Allergy, 66 (2011):523-524,
https://hdl.handle.net/21.15107/rcub_cherry_1473 .