TY  - JOUR
AU  - Dragačević, Luka
AU  - Lopandić, Zorana
AU  - Gavrović-Jankulović, Marija
AU  - Živković, Irena
AU  - Blagojević, Veljko
AU  - Polović, Natalija
AU  - Minić, Rajna
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4887
AB  - The surface of microorganisms is covered with carbohydrates, which makes them unique, self-sustaining glycan probes. Lectins are able to bind to these probes, and this interaction can be exploited for selecting microorganisms or novel lectins. To examine lectin-microorganism interactions, we have previously developed an enzyme-linked lectin sorbent assay (ELLSA) with whole bacterial cells. To further test the validity of this methodology, here we compare it with flow cytometry. For this purpose, we used biotinylated recombinantly produced lectin from Musa acuminata (BanLec), this lectin’s recombinantly produced chimera with green fluorescent protein (BanLec-eGFP) and a lectin from Ricinus communis (RCA120), both biotinylated and FITC labeled. Parallel testing showed equivalent results for the two methods, in terms of the presence or absence of binding, with signal intensity yielding high Pearson correlation coefficient of 0.8 for BanLec and 0.95 for RCA120. The ELLSA method demonstrated multiple advantages, such as reliability and convenience for high-throughput analysis; it also required less lectin and yielded more consistent results. As such, ELLSA proved to be a useful tool for profiling microbial glycan structures or testing novel lectins.
PB  - Springer
T2  - Applied Biochemistry and Biotechnology
T2  - Applied Biochemistry and BiotechnologyAppl Biochem Biotechnol
T1  - Comparison of Enzyme-Linked Lectin Sorbent Assay
and Flow Cytometry for Profling Microbial Glycans
VL  - 194
SP  - 2047
EP  - 2060
DO  - 10.1007/s12010-021-03772-w
ER  - 

@article{
author = "Dragačević, Luka and Lopandić, Zorana and Gavrović-Jankulović, Marija and Živković, Irena and Blagojević, Veljko and Polović, Natalija and Minić, Rajna",
year = "2022",
abstract = "The surface of microorganisms is covered with carbohydrates, which makes them unique, self-sustaining glycan probes. Lectins are able to bind to these probes, and this interaction can be exploited for selecting microorganisms or novel lectins. To examine lectin-microorganism interactions, we have previously developed an enzyme-linked lectin sorbent assay (ELLSA) with whole bacterial cells. To further test the validity of this methodology, here we compare it with flow cytometry. For this purpose, we used biotinylated recombinantly produced lectin from Musa acuminata (BanLec), this lectin’s recombinantly produced chimera with green fluorescent protein (BanLec-eGFP) and a lectin from Ricinus communis (RCA120), both biotinylated and FITC labeled. Parallel testing showed equivalent results for the two methods, in terms of the presence or absence of binding, with signal intensity yielding high Pearson correlation coefficient of 0.8 for BanLec and 0.95 for RCA120. The ELLSA method demonstrated multiple advantages, such as reliability and convenience for high-throughput analysis; it also required less lectin and yielded more consistent results. As such, ELLSA proved to be a useful tool for profiling microbial glycan structures or testing novel lectins.",
publisher = "Springer",
journal = "Applied Biochemistry and Biotechnology, Applied Biochemistry and BiotechnologyAppl Biochem Biotechnol",
title = "Comparison of Enzyme-Linked Lectin Sorbent Assay
and Flow Cytometry for Profling Microbial Glycans",
volume = "194",
pages = "2047-2060",
doi = "10.1007/s12010-021-03772-w"
}

Dragačević, L., Lopandić, Z., Gavrović-Jankulović, M., Živković, I., Blagojević, V., Polović, N.,& Minić, R.. (2022). Comparison of Enzyme-Linked Lectin Sorbent Assay
and Flow Cytometry for Profling Microbial Glycans. in Applied Biochemistry and Biotechnology
Springer., 194, 2047-2060.
https://doi.org/10.1007/s12010-021-03772-w

Dragačević L, Lopandić Z, Gavrović-Jankulović M, Živković I, Blagojević V, Polović N, Minić R. Comparison of Enzyme-Linked Lectin Sorbent Assay
and Flow Cytometry for Profling Microbial Glycans. in Applied Biochemistry and Biotechnology. 2022;194:2047-2060.
doi:10.1007/s12010-021-03772-w .

Dragačević, Luka, Lopandić, Zorana, Gavrović-Jankulović, Marija, Živković, Irena, Blagojević, Veljko, Polović, Natalija, Minić, Rajna, "Comparison of Enzyme-Linked Lectin Sorbent Assay
and Flow Cytometry for Profling Microbial Glycans" in Applied Biochemistry and Biotechnology, 194 (2022):2047-2060,
https://doi.org/10.1007/s12010-021-03772-w . .

TY  - DATA
AU  - Dragačević, Luka
AU  - Lopandić, Zorana
AU  - Gavrović-Jankulović, Marija
AU  - Živković, Irena
AU  - Blagojević, Veljko
AU  - Polović, Natalija
AU  - Minić, Rajna
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4888
PB  - Springer
T2  - Applied Biochemistry and Biotechnology
T1  - Supplementary data for the article: Dragačević, L.; Lopandić, Z.; Gavrović-Jankulović, M.; Živković, I.; Blagojević, V.; Polović, N.; Minić, R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. Appl Biochem Biotechnol 2022. https://doi.org/10.1007/s12010-021-03772-w.
VL  - 194
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4888
ER  - 

@misc{
author = "Dragačević, Luka and Lopandić, Zorana and Gavrović-Jankulović, Marija and Živković, Irena and Blagojević, Veljko and Polović, Natalija and Minić, Rajna",
year = "2022",
publisher = "Springer",
journal = "Applied Biochemistry and Biotechnology",
title = "Supplementary data for the article: Dragačević, L.; Lopandić, Z.; Gavrović-Jankulović, M.; Živković, I.; Blagojević, V.; Polović, N.; Minić, R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. Appl Biochem Biotechnol 2022. https://doi.org/10.1007/s12010-021-03772-w.",
volume = "194",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4888"
}

Dragačević, L., Lopandić, Z., Gavrović-Jankulović, M., Živković, I., Blagojević, V., Polović, N.,& Minić, R.. (2022). Supplementary data for the article: Dragačević, L.; Lopandić, Z.; Gavrović-Jankulović, M.; Živković, I.; Blagojević, V.; Polović, N.; Minić, R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. Appl Biochem Biotechnol 2022. https://doi.org/10.1007/s12010-021-03772-w.. in Applied Biochemistry and Biotechnology
Springer., 194.
https://hdl.handle.net/21.15107/rcub_cherry_4888

Dragačević L, Lopandić Z, Gavrović-Jankulović M, Živković I, Blagojević V, Polović N, Minić R. Supplementary data for the article: Dragačević, L.; Lopandić, Z.; Gavrović-Jankulović, M.; Živković, I.; Blagojević, V.; Polović, N.; Minić, R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. Appl Biochem Biotechnol 2022. https://doi.org/10.1007/s12010-021-03772-w.. in Applied Biochemistry and Biotechnology. 2022;194.
https://hdl.handle.net/21.15107/rcub_cherry_4888 .

Dragačević, Luka, Lopandić, Zorana, Gavrović-Jankulović, Marija, Živković, Irena, Blagojević, Veljko, Polović, Natalija, Minić, Rajna, "Supplementary data for the article: Dragačević, L.; Lopandić, Z.; Gavrović-Jankulović, M.; Živković, I.; Blagojević, V.; Polović, N.; Minić, R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. Appl Biochem Biotechnol 2022. https://doi.org/10.1007/s12010-021-03772-w." in Applied Biochemistry and Biotechnology, 194 (2022),
https://hdl.handle.net/21.15107/rcub_cherry_4888 .

TY  - JOUR
AU  - Milovanović, Vladimir
AU  - Minić, Rajna
AU  - Vakić, Jelena
AU  - Ivanović, Saša
AU  - Čupić, Vitomir
AU  - Borozan, Sunćica
AU  - Nešić, Andrijana N.
AU  - Živković, Irena
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0041010121000362
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4490
AB  - The MTT assay is routinely used to detect the activity of living cells. While working with Vipera ammodytes venom we detected the reduction of MTT without the presence of cells, in a concentration-dependent manner. By combining non-reducing PAGE, L-amino acid oxidase (LAAO) assays, and standard MTT assays, we established and confirmed that venom MTT reduction is catalyzed by only one enzyme, the LAAO. Even though it was previously known that the dimeric and tetrameric forms of LAAO are active, we conclude that the enzyme is also active in the monomeric form. Our results have led to the definition of a new MTT assay in a microtiter plate for in vitro testing of svLAAO activity i.e. from the venom of the V. ammodytes snake. Potentially, this method can be used for testing hemorrhagic venoms of other snakes as well as the LAAO neutralization capability of appropriate antivenoms.
PB  - Elsevier
T2  - Toxicon
T2  - ToxiconToxicon
T1  - MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation
VL  - 192
SP  - 57
EP  - 65
DO  - 10.1016/j.toxicon.2021.01.012
ER  - 

@article{
author = "Milovanović, Vladimir and Minić, Rajna and Vakić, Jelena and Ivanović, Saša and Čupić, Vitomir and Borozan, Sunćica and Nešić, Andrijana N. and Živković, Irena",
year = "2021",
abstract = "The MTT assay is routinely used to detect the activity of living cells. While working with Vipera ammodytes venom we detected the reduction of MTT without the presence of cells, in a concentration-dependent manner. By combining non-reducing PAGE, L-amino acid oxidase (LAAO) assays, and standard MTT assays, we established and confirmed that venom MTT reduction is catalyzed by only one enzyme, the LAAO. Even though it was previously known that the dimeric and tetrameric forms of LAAO are active, we conclude that the enzyme is also active in the monomeric form. Our results have led to the definition of a new MTT assay in a microtiter plate for in vitro testing of svLAAO activity i.e. from the venom of the V. ammodytes snake. Potentially, this method can be used for testing hemorrhagic venoms of other snakes as well as the LAAO neutralization capability of appropriate antivenoms.",
publisher = "Elsevier",
journal = "Toxicon, ToxiconToxicon",
title = "MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation",
volume = "192",
pages = "57-65",
doi = "10.1016/j.toxicon.2021.01.012"
}

Milovanović, V., Minić, R., Vakić, J., Ivanović, S., Čupić, V., Borozan, S., Nešić, A. N.,& Živković, I.. (2021). MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation. in Toxicon
Elsevier., 192, 57-65.
https://doi.org/10.1016/j.toxicon.2021.01.012

Milovanović V, Minić R, Vakić J, Ivanović S, Čupić V, Borozan S, Nešić AN, Živković I. MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation. in Toxicon. 2021;192:57-65.
doi:10.1016/j.toxicon.2021.01.012 .

Milovanović, Vladimir, Minić, Rajna, Vakić, Jelena, Ivanović, Saša, Čupić, Vitomir, Borozan, Sunćica, Nešić, Andrijana N., Živković, Irena, "MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation" in Toxicon, 192 (2021):57-65,
https://doi.org/10.1016/j.toxicon.2021.01.012 . .

TY  - JOUR
AU  - Lopandić, Zorana
AU  - Dragačević, Luka
AU  - Popović, Dragan M.
AU  - Anđelković, Uroš
AU  - Minić, Rajna
AU  - Gavrović-Jankulović, Marija
PY  - 2021
UR  - https://www.mdpi.com/2218-273X/11/2/180
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4489
AB  - Fluorescently labeled lectins are useful tools for in vivo and in vitro studies of the structure and function of tissues and various pathogens such as viruses, bacteria, and fungi. For the evaluation of high-mannose glycans present on various glycoproteins, a three-dimensional (3D) model of the chimera was designed from the crystal structures of recombinant banana lectin (BanLec, Protein Data Bank entry (PDB): 5EXG) and an enhanced green fluorescent protein (eGFP, PDB 4EUL) by applying molecular modeling and molecular mechanics and expressed in Escherichia coli. BanLec-eGFP, produced as a soluble cytosolic protein of about 42 kDa, revealed β-sheets (41%) as the predominant secondary structures, with the emission peak maximum detected at 509 nm (excitation wavelength 488 nm). More than 65% of the primary structure was confirmed by mass spectrometry. Competitive BanLec-eGFP binding to high mannose glycans of the influenza vaccine (Vaxigrip®) was shown in a fluorescence-linked lectin sorbent assay (FLLSA) with monosaccharides (mannose and glucose) and wild type BanLec and H84T BanLec mutant. BanLec-eGFP exhibited binding to mannose residues on different strains of Salmonella in flow cytometry, with especially pronounced binding to a Salmonella Typhi clinical isolate. BanLec-eGFP can be a useful tool for screening high-mannose glycosylation sites on different microorganisms.
PB  - MDPI
T2  - Biomolecules
T2  - Biomolecules
T1  - BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms
VL  - 11
IS  - 2
SP  - 180
DO  - 10.3390/biom11020180
ER  - 

@article{
author = "Lopandić, Zorana and Dragačević, Luka and Popović, Dragan M. and Anđelković, Uroš and Minić, Rajna and Gavrović-Jankulović, Marija",
year = "2021",
abstract = "Fluorescently labeled lectins are useful tools for in vivo and in vitro studies of the structure and function of tissues and various pathogens such as viruses, bacteria, and fungi. For the evaluation of high-mannose glycans present on various glycoproteins, a three-dimensional (3D) model of the chimera was designed from the crystal structures of recombinant banana lectin (BanLec, Protein Data Bank entry (PDB): 5EXG) and an enhanced green fluorescent protein (eGFP, PDB 4EUL) by applying molecular modeling and molecular mechanics and expressed in Escherichia coli. BanLec-eGFP, produced as a soluble cytosolic protein of about 42 kDa, revealed β-sheets (41%) as the predominant secondary structures, with the emission peak maximum detected at 509 nm (excitation wavelength 488 nm). More than 65% of the primary structure was confirmed by mass spectrometry. Competitive BanLec-eGFP binding to high mannose glycans of the influenza vaccine (Vaxigrip®) was shown in a fluorescence-linked lectin sorbent assay (FLLSA) with monosaccharides (mannose and glucose) and wild type BanLec and H84T BanLec mutant. BanLec-eGFP exhibited binding to mannose residues on different strains of Salmonella in flow cytometry, with especially pronounced binding to a Salmonella Typhi clinical isolate. BanLec-eGFP can be a useful tool for screening high-mannose glycosylation sites on different microorganisms.",
publisher = "MDPI",
journal = "Biomolecules, Biomolecules",
title = "BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms",
volume = "11",
number = "2",
pages = "180",
doi = "10.3390/biom11020180"
}

Lopandić, Z., Dragačević, L., Popović, D. M., Anđelković, U., Minić, R.,& Gavrović-Jankulović, M.. (2021). BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms. in Biomolecules
MDPI., 11(2), 180.
https://doi.org/10.3390/biom11020180

Lopandić Z, Dragačević L, Popović DM, Anđelković U, Minić R, Gavrović-Jankulović M. BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms. in Biomolecules. 2021;11(2):180.
doi:10.3390/biom11020180 .

Lopandić, Zorana, Dragačević, Luka, Popović, Dragan M., Anđelković, Uroš, Minić, Rajna, Gavrović-Jankulović, Marija, "BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms" in Biomolecules, 11, no. 2 (2021):180,
https://doi.org/10.3390/biom11020180 . .

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  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Popović, Dragan M.
AU  - Živković, Irena
AU  - Gavrović-Jankulović, Marija
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2236
AB  - Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Life Sciences
T1  - Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy
VL  - 213
SP  - 158
EP  - 165
DO  - 10.1016/j.lfs.2018.10.036
ER  - 

@article{
author = "Mrkić, Ivan and Minić, Rajna and Popović, Dragan M. and Živković, Irena and Gavrović-Jankulović, Marija",
year = "2018",
abstract = "Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Life Sciences",
title = "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy",
volume = "213",
pages = "158-165",
doi = "10.1016/j.lfs.2018.10.036"
}

Mrkić, I., Minić, R., Popović, D. M., Živković, I.,& Gavrović-Jankulović, M.. (2018). Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences
Pergamon-Elsevier Science Ltd, Oxford., 213, 158-165.
https://doi.org/10.1016/j.lfs.2018.10.036

Mrkić I, Minić R, Popović DM, Živković I, Gavrović-Jankulović M. Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences. 2018;213:158-165.
doi:10.1016/j.lfs.2018.10.036 .

Mrkić, Ivan, Minić, Rajna, Popović, Dragan M., Živković, Irena, Gavrović-Jankulović, Marija, "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy" in Life Sciences, 213 (2018):158-165,
https://doi.org/10.1016/j.lfs.2018.10.036 . .

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Popović, Dragan M.
AU  - Živković, Irena
AU  - Gavrović-Jankulović, Marija
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2887
AB  - Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.
PB  - Elsevier
T2  - Life Sciences
T1  - Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy
VL  - 213
SP  - 158
EP  - 165
DO  - 10.1016/j.lfs.2018.10.036
ER  - 

@article{
author = "Mrkić, Ivan and Minić, Rajna and Popović, Dragan M. and Živković, Irena and Gavrović-Jankulović, Marija",
year = "2018",
abstract = "Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.",
publisher = "Elsevier",
journal = "Life Sciences",
title = "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy",
volume = "213",
pages = "158-165",
doi = "10.1016/j.lfs.2018.10.036"
}

Mrkić, I., Minić, R., Popović, D. M., Živković, I.,& Gavrović-Jankulović, M.. (2018). Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences
Elsevier., 213, 158-165.
https://doi.org/10.1016/j.lfs.2018.10.036

Mrkić I, Minić R, Popović DM, Živković I, Gavrović-Jankulović M. Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences. 2018;213:158-165.
doi:10.1016/j.lfs.2018.10.036 .

Mrkić, Ivan, Minić, Rajna, Popović, Dragan M., Živković, Irena, Gavrović-Jankulović, Marija, "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy" in Life Sciences, 213 (2018):158-165,
https://doi.org/10.1016/j.lfs.2018.10.036 . .

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Bulat, Tanja
AU  - Aradska, Jana
AU  - Atanasković-Marković, Marina
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2472
AB  - BACKGROUND: Group 1 and group 2 allergens from house dust mite are the major elicitors of respiratory allergic diseases and the main candidates for immunotherapy. RESULTS: The potential therapeutic role of a chimera composed of recombinant Der p 2 (D2) linked to Influenza A virus hemagglutinin 1 (H1) for intranasal application was created, expressed and tested in a mouse model. H1D2 and D2 were produced by genetic engineering in Escherichia coli and their primary structure was confirmed by mass fingerprint. Both antigens preserved IgE reactivity in immunoblot with serum from seven house dust mite allergic persons. Balb/c mice were sensitized with D2 allergen in alum and subsequently received H1D2 or D2, intranasally. The reduced levels of serum D2 specific IgE, together with the increased serum specific IgG and IgA were detected in both groups which received H1D2 and D2 intranasally. A higher level of effector CD4+CD25+ spleen lymphocytes was found only in the group of mice which received i.n. H1D2. CONCLUSION: H1D2 chimera can have therapeutic potential in Der p 2 allergic persons as dual vaccine which, beside protective allergen specific, can provide protective antibodies against Influenza A virus hemagglutinin 1. (C) 2016 Society of Chemical Industry
PB  - Wiley, Hoboken
T2  - Journal of Chemical Technology and Biotechnology
T1  - Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera
VL  - 92
IS  - 6
SP  - 1328
EP  - 1335
DO  - 10.1002/jctb.5127
ER  - 

@article{
author = "Mrkić, Ivan and Minić, Rajna and Bulat, Tanja and Aradska, Jana and Atanasković-Marković, Marina and Drakulić, Branko J. and Gavrović-Jankulović, Marija",
year = "2017",
abstract = "BACKGROUND: Group 1 and group 2 allergens from house dust mite are the major elicitors of respiratory allergic diseases and the main candidates for immunotherapy. RESULTS: The potential therapeutic role of a chimera composed of recombinant Der p 2 (D2) linked to Influenza A virus hemagglutinin 1 (H1) for intranasal application was created, expressed and tested in a mouse model. H1D2 and D2 were produced by genetic engineering in Escherichia coli and their primary structure was confirmed by mass fingerprint. Both antigens preserved IgE reactivity in immunoblot with serum from seven house dust mite allergic persons. Balb/c mice were sensitized with D2 allergen in alum and subsequently received H1D2 or D2, intranasally. The reduced levels of serum D2 specific IgE, together with the increased serum specific IgG and IgA were detected in both groups which received H1D2 and D2 intranasally. A higher level of effector CD4+CD25+ spleen lymphocytes was found only in the group of mice which received i.n. H1D2. CONCLUSION: H1D2 chimera can have therapeutic potential in Der p 2 allergic persons as dual vaccine which, beside protective allergen specific, can provide protective antibodies against Influenza A virus hemagglutinin 1. (C) 2016 Society of Chemical Industry",
publisher = "Wiley, Hoboken",
journal = "Journal of Chemical Technology and Biotechnology",
title = "Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera",
volume = "92",
number = "6",
pages = "1328-1335",
doi = "10.1002/jctb.5127"
}

Mrkić, I., Minić, R., Bulat, T., Aradska, J., Atanasković-Marković, M., Drakulić, B. J.,& Gavrović-Jankulović, M.. (2017). Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera. in Journal of Chemical Technology and Biotechnology
Wiley, Hoboken., 92(6), 1328-1335.
https://doi.org/10.1002/jctb.5127

Mrkić I, Minić R, Bulat T, Aradska J, Atanasković-Marković M, Drakulić BJ, Gavrović-Jankulović M. Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera. in Journal of Chemical Technology and Biotechnology. 2017;92(6):1328-1335.
doi:10.1002/jctb.5127 .

Mrkić, Ivan, Minić, Rajna, Bulat, Tanja, Aradska, Jana, Atanasković-Marković, Marina, Drakulić, Branko J., Gavrović-Jankulović, Marija, "Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera" in Journal of Chemical Technology and Biotechnology, 92, no. 6 (2017):1328-1335,
https://doi.org/10.1002/jctb.5127 . .

TY  - JOUR
AU  - Minić, Rajna
AU  - Gavrović-Jankulović, Marija
AU  - Petrusic, Vladimir
AU  - Živković, Irena
AU  - Eijsink, Vincent G. H.
AU  - Dimitrijevic, Ljiljana
AU  - Mathiesen, Geir
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1681
AB  - Group I grass pollen allergens are major contributors to grass pollen-related seasonal allergic rhinitis, and as such a primary target for allergen specific immunotherapy. In this study the potential therapeutic role of oral application of Lactobacillus plantarum WCFS1, directing cell wall attachment of the recombinant Fes p1 allergen, from Festuca pratensis was tested in a mouse model of Fes p1 allergy. For surface expression of Fes p1 allergen in L. plantarum WCFS1 pSIP system with inducible expression was used. Balb/c mice were sensitized with Fes p1 protein in alum and subsequently received live recombinant L. plantarum orally. Antibody levels (IgE, total IgG, IgG1, IgG2a, and IgA) were determined by ELISA. Differential eosinophil count in peripheral blood was performed. Reduced peripheral blood eosinophilia and increased serum IgG2A levels was detected in both groups which received live L. plantarum orally. Specific serum IgA levels were increased only in mice treated with the recombinant bacteria. Oral application of L. plantarum WCFS1 has a beneficial therapeutic effect in a mouse model of Fes p1 allergy. Cell surface expression of Fes p1 allergen potentiates this phenomenon in an allergen specific way. (C) 2015 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Biotechnology
T1  - Effects of orally applied Fes p1-displaying L. plantarum WCFS1 on Fes p1 induced allergy in mice
VL  - 199
SP  - 23
EP  - 28
DO  - 10.1016/j.jbiotec.2015.01.028
ER  - 

@article{
author = "Minić, Rajna and Gavrović-Jankulović, Marija and Petrusic, Vladimir and Živković, Irena and Eijsink, Vincent G. H. and Dimitrijevic, Ljiljana and Mathiesen, Geir",
year = "2015",
abstract = "Group I grass pollen allergens are major contributors to grass pollen-related seasonal allergic rhinitis, and as such a primary target for allergen specific immunotherapy. In this study the potential therapeutic role of oral application of Lactobacillus plantarum WCFS1, directing cell wall attachment of the recombinant Fes p1 allergen, from Festuca pratensis was tested in a mouse model of Fes p1 allergy. For surface expression of Fes p1 allergen in L. plantarum WCFS1 pSIP system with inducible expression was used. Balb/c mice were sensitized with Fes p1 protein in alum and subsequently received live recombinant L. plantarum orally. Antibody levels (IgE, total IgG, IgG1, IgG2a, and IgA) were determined by ELISA. Differential eosinophil count in peripheral blood was performed. Reduced peripheral blood eosinophilia and increased serum IgG2A levels was detected in both groups which received live L. plantarum orally. Specific serum IgA levels were increased only in mice treated with the recombinant bacteria. Oral application of L. plantarum WCFS1 has a beneficial therapeutic effect in a mouse model of Fes p1 allergy. Cell surface expression of Fes p1 allergen potentiates this phenomenon in an allergen specific way. (C) 2015 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Biotechnology",
title = "Effects of orally applied Fes p1-displaying L. plantarum WCFS1 on Fes p1 induced allergy in mice",
volume = "199",
pages = "23-28",
doi = "10.1016/j.jbiotec.2015.01.028"
}

Minić, R., Gavrović-Jankulović, M., Petrusic, V., Živković, I., Eijsink, V. G. H., Dimitrijevic, L.,& Mathiesen, G.. (2015). Effects of orally applied Fes p1-displaying L. plantarum WCFS1 on Fes p1 induced allergy in mice. in Journal of Biotechnology
Elsevier Science Bv, Amsterdam., 199, 23-28.
https://doi.org/10.1016/j.jbiotec.2015.01.028

Minić R, Gavrović-Jankulović M, Petrusic V, Živković I, Eijsink VGH, Dimitrijevic L, Mathiesen G. Effects of orally applied Fes p1-displaying L. plantarum WCFS1 on Fes p1 induced allergy in mice. in Journal of Biotechnology. 2015;199:23-28.
doi:10.1016/j.jbiotec.2015.01.028 .

Minić, Rajna, Gavrović-Jankulović, Marija, Petrusic, Vladimir, Živković, Irena, Eijsink, Vincent G. H., Dimitrijevic, Ljiljana, Mathiesen, Geir, "Effects of orally applied Fes p1-displaying L. plantarum WCFS1 on Fes p1 induced allergy in mice" in Journal of Biotechnology, 199 (2015):23-28,
https://doi.org/10.1016/j.jbiotec.2015.01.028 . .