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  - 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  - 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 . .

TY  - JOUR
AU  - Stojanović, Marijana M.
AU  - Živković, Irena
AU  - Petrusic, Vladimir Z.
AU  - Kosec, Dusko J.
AU  - Dimitrijevic, Rajna D.
AU  - Jankov, Ratko M.
AU  - Dimitrijevic, Ljijana A.
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1043
AB  - Lectins are widely used in many types of assay but some lectins such as banana lectin (BanLec) are recognised as potent immunostimulators Although BanLec's structure and binding characteristics are now familiar, its immunostimulatory potential has not yet been fully explored The synthesis by recombinant technology of a BanLec isoform (rBanLec) whose binding properties are similar to its natural counterpart has made it possible to overcome the twin problems of natural BanLec's microheterogeneity and low availability This study's aim is to explore the immunostimulatory potential of rBanLec in the murine model Analyses of the responses of Balb/c- and C57 BL/6-originated splenocytes to in vitro rBanLec stimulation were performed to examine the dependency of rBanLec's immunostimulatory potential upon the splenocytes' genetic background It is shown that the responses of Balb/c- and C57 BL/6-originated splenocytes to rBanLec stimulation differ both qualitatively and in intensity. The hallmarks of the induced responses are T lymphocyte proliferation and intensive interferon-gamma secretion Both phenomena are more marked in Balb/c-originated cultures; Balb/c-originated lymphocytes produce interleukin (IL)-4 and IL-10 following rBanLec stimulation Out results demonstrate that any responses to rBanLec stimulation are highly dependent upon genetic background. they suggest that genetic background must be an important consideration in any further investigations using animal models or when exploring rBanLec's potential human applications (C) 2009 Elsevier B V. All rights reserved
PB  - Elsevier Science Bv, Amsterdam
T2  - International Immunopharmacology
T1  - In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma
VL  - 10
IS  - 1
SP  - 120
EP  - 129
DO  - 10.1016/j.intimp.2009.10.007
ER  - 

@article{
author = "Stojanović, Marijana M. and Živković, Irena and Petrusic, Vladimir Z. and Kosec, Dusko J. and Dimitrijevic, Rajna D. and Jankov, Ratko M. and Dimitrijevic, Ljijana A. and Gavrović-Jankulović, Marija",
year = "2010",
abstract = "Lectins are widely used in many types of assay but some lectins such as banana lectin (BanLec) are recognised as potent immunostimulators Although BanLec's structure and binding characteristics are now familiar, its immunostimulatory potential has not yet been fully explored The synthesis by recombinant technology of a BanLec isoform (rBanLec) whose binding properties are similar to its natural counterpart has made it possible to overcome the twin problems of natural BanLec's microheterogeneity and low availability This study's aim is to explore the immunostimulatory potential of rBanLec in the murine model Analyses of the responses of Balb/c- and C57 BL/6-originated splenocytes to in vitro rBanLec stimulation were performed to examine the dependency of rBanLec's immunostimulatory potential upon the splenocytes' genetic background It is shown that the responses of Balb/c- and C57 BL/6-originated splenocytes to rBanLec stimulation differ both qualitatively and in intensity. The hallmarks of the induced responses are T lymphocyte proliferation and intensive interferon-gamma secretion Both phenomena are more marked in Balb/c-originated cultures; Balb/c-originated lymphocytes produce interleukin (IL)-4 and IL-10 following rBanLec stimulation Out results demonstrate that any responses to rBanLec stimulation are highly dependent upon genetic background. they suggest that genetic background must be an important consideration in any further investigations using animal models or when exploring rBanLec's potential human applications (C) 2009 Elsevier B V. All rights reserved",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "International Immunopharmacology",
title = "In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma",
volume = "10",
number = "1",
pages = "120-129",
doi = "10.1016/j.intimp.2009.10.007"
}

Stojanović, M. M., Živković, I., Petrusic, V. Z., Kosec, D. J., Dimitrijevic, R. D., Jankov, R. M., Dimitrijevic, L. A.,& Gavrović-Jankulović, M.. (2010). In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma. in International Immunopharmacology
Elsevier Science Bv, Amsterdam., 10(1), 120-129.
https://doi.org/10.1016/j.intimp.2009.10.007

Stojanović MM, Živković I, Petrusic VZ, Kosec DJ, Dimitrijevic RD, Jankov RM, Dimitrijevic LA, Gavrović-Jankulović M. In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma. in International Immunopharmacology. 2010;10(1):120-129.
doi:10.1016/j.intimp.2009.10.007 .

Stojanović, Marijana M., Živković, Irena, Petrusic, Vladimir Z., Kosec, Dusko J., Dimitrijevic, Rajna D., Jankov, Ratko M., Dimitrijevic, Ljijana A., Gavrović-Jankulović, Marija, "In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma" in International Immunopharmacology, 10, no. 1 (2010):120-129,
https://doi.org/10.1016/j.intimp.2009.10.007 . .