TY  - JOUR
AU  - Lopandić, Zorana
AU  - Dragačević, Luka
AU  - Kosanović, Dejana
AU  - Burazer, Lidija
AU  - Gavrović-Jankulović, Marija
AU  - Minić, Rajna
PY  - 2022
UR  - http://intor.torlakinstitut.com/handle/123456789/787
AB  - In vivo animal models can provide worthy information on various aspects of asthma mechanism and pathogenesis. The genetic predisposition and phenotype of mice may affect the immune response itself. Here we compare the early immune response to Der p 2 or HDM allergen extract upon injection and inhalation in BALB/c and C57BL/6 mice. Female C57BL/6 and BALB/c mice were immunized with Der p 2 allergen subcutaneously followed by inhalation of Der p 2 or HDM extract. After challenge, the mice were euthanized; blood, bronchoalveolar lavage (BAL), spleens and lungs were collected. Cells from BAL were identified by May-Grünwald Giemsa staining and lung leukocyte populations were analyzed by flow cytometry. Serum antibody levels of Der p 2 specific IgE, IgG, IgG1 and IgG2a were assessed by ELISA, and cytokine secretion (IL-4, IFN-γ and IL-10) was evaluated upon stimulation with Der p 2 or HDM extract. The Th2 immune response was confirmed by elevated allergen-specific immunoglobulin E (IgE) and the allergic reaction was evidenced by infiltration of eosinophils and/or neutrophils into BAL. We found that BALB/c mice were inefficient in integrating local with systemic immune response, evidenced by almost no IgG or IgE production upon one subcutaneous injection and subsequent inhalation of Der p 2 allergen; also, the bronchoalveolar lavage infiltrate in these mice consisted of neutrophil infiltration, unlike C57BL/6 mice in which eosinophilic infiltrate predominated. The differences between BALB/c and C57BL/6 mice strains could be exploited for generating different types of responses to the Der p 2 allergen.
PB  - Elsevier
T2  - Journal of Immunological Methods
T2  - Journal of Immunological MethodsJournal of Immunological Methods
T1  - Differences in mouse strains determine the outcome of Der p 2 allergy induction protocols
SP  - 113382
VL  - 511
DO  - 10.1016/j.jim.2022.113382
ER  - 

@article{
author = "Lopandić, Zorana and Dragačević, Luka and Kosanović, Dejana and Burazer, Lidija and Gavrović-Jankulović, Marija and Minić, Rajna",
year = "2022",
abstract = "In vivo animal models can provide worthy information on various aspects of asthma mechanism and pathogenesis. The genetic predisposition and phenotype of mice may affect the immune response itself. Here we compare the early immune response to Der p 2 or HDM allergen extract upon injection and inhalation in BALB/c and C57BL/6 mice. Female C57BL/6 and BALB/c mice were immunized with Der p 2 allergen subcutaneously followed by inhalation of Der p 2 or HDM extract. After challenge, the mice were euthanized; blood, bronchoalveolar lavage (BAL), spleens and lungs were collected. Cells from BAL were identified by May-Grünwald Giemsa staining and lung leukocyte populations were analyzed by flow cytometry. Serum antibody levels of Der p 2 specific IgE, IgG, IgG1 and IgG2a were assessed by ELISA, and cytokine secretion (IL-4, IFN-γ and IL-10) was evaluated upon stimulation with Der p 2 or HDM extract. The Th2 immune response was confirmed by elevated allergen-specific immunoglobulin E (IgE) and the allergic reaction was evidenced by infiltration of eosinophils and/or neutrophils into BAL. We found that BALB/c mice were inefficient in integrating local with systemic immune response, evidenced by almost no IgG or IgE production upon one subcutaneous injection and subsequent inhalation of Der p 2 allergen; also, the bronchoalveolar lavage infiltrate in these mice consisted of neutrophil infiltration, unlike C57BL/6 mice in which eosinophilic infiltrate predominated. The differences between BALB/c and C57BL/6 mice strains could be exploited for generating different types of responses to the Der p 2 allergen.",
publisher = "Elsevier",
journal = "Journal of Immunological Methods, Journal of Immunological MethodsJournal of Immunological Methods",
title = "Differences in mouse strains determine the outcome of Der p 2 allergy induction protocols",
pages = "113382",
volume = "511",
doi = "10.1016/j.jim.2022.113382"
}

Lopandić, Z., Dragačević, L., Kosanović, D., Burazer, L., Gavrović-Jankulović, M.,& Minić, R.. (2022). Differences in mouse strains determine the outcome of Der p 2 allergy induction protocols. in Journal of Immunological Methods
Elsevier., 511, 113382.
https://doi.org/10.1016/j.jim.2022.113382

Lopandić Z, Dragačević L, Kosanović D, Burazer L, Gavrović-Jankulović M, Minić R. Differences in mouse strains determine the outcome of Der p 2 allergy induction protocols. in Journal of Immunological Methods. 2022;511:113382.
doi:10.1016/j.jim.2022.113382 .

Lopandić, Zorana, Dragačević, Luka, Kosanović, Dejana, Burazer, Lidija, Gavrović-Jankulović, Marija, Minić, Rajna, "Differences in mouse strains determine the outcome of Der p 2 allergy induction protocols" in Journal of Immunological Methods, 511 (2022):113382,
https://doi.org/10.1016/j.jim.2022.113382 . .

TY  - JOUR
AU  - Nikodijević, Slavomir
AU  - Blagojević, Veljko
AU  - Ćuruvija, Ivana
AU  - Kosanović, Dejana
AU  - Đukić, Tamara
AU  - Đorđević, Brižita
AU  - Ilić, Vesna
AU  - Minić, Rajna
PY  - 2022
UR  - http://intor.torlakinstitut.com/handle/123456789/632
AB  - Increased interest in microbiota calls for the thorough analysis of antibody reactivity to different microorganisms. As salivary IgA represents the first line of defence against microorganisms contacting mucosal surfaces, we explored the binding and specificity of salivary IgA by testing the binding of purified, FITC-labelled salivary IgA to different microorganisms in flow cytometry and conclude that this kind of analysis enables the differentiation of species/strains with high IgA binding capacity, which should be corroborated on a larger sample size. Further we compare, with in-house ELISA, the binding of polyclonal salivary IgA with the binding of polyclonal serum IgA from the same individuals to whole microbial cells and to purified microbial components. High correlations were obtained in total salivary IgA binding to Lactobacillus rhamnosus and Escherichia coli, very distant bacterial species, as well as to isolated bacterial components (r = .70–.97). The binding of total salivary IgA resembled the binding of both salivary IgA1 and IgA2, with IgA2 predominating. For serum polyclonal IgA repertoire, substantially higher specificity was obtained. Serum IgA binding to E. coli correlated best with serum IgA binding to lipopolysaccharide (r = .86), and serum IgA against L. rhamnosus correlated best with the anti-peptidoglycan IgA levels (r = .88). We have also detected that total serum IgA response is governed by either IgA1 or IgA2 response, depending on the nature of the antigen/s. We conclude that steady state salivary IgA repertoire, unlike serum IgA repertoire, consists of polyreactive antibodies with innate specificity, questioning its capacity to select resident microbiota.
PB  - The Scandinavian Foundation for Immunology
T2  - Scandinavian Journal of Immunology
T1  - Selectivity of polyclonal repertoire of anti-microbial IgA and its subclasses in saliva and serum in humans
VL  - 96
DO  - 10.1111/sji.13223
ER  - 

@article{
author = "Nikodijević, Slavomir and Blagojević, Veljko and Ćuruvija, Ivana and Kosanović, Dejana and Đukić, Tamara and Đorđević, Brižita and Ilić, Vesna and Minić, Rajna",
year = "2022",
abstract = "Increased interest in microbiota calls for the thorough analysis of antibody reactivity to different microorganisms. As salivary IgA represents the first line of defence against microorganisms contacting mucosal surfaces, we explored the binding and specificity of salivary IgA by testing the binding of purified, FITC-labelled salivary IgA to different microorganisms in flow cytometry and conclude that this kind of analysis enables the differentiation of species/strains with high IgA binding capacity, which should be corroborated on a larger sample size. Further we compare, with in-house ELISA, the binding of polyclonal salivary IgA with the binding of polyclonal serum IgA from the same individuals to whole microbial cells and to purified microbial components. High correlations were obtained in total salivary IgA binding to Lactobacillus rhamnosus and Escherichia coli, very distant bacterial species, as well as to isolated bacterial components (r = .70–.97). The binding of total salivary IgA resembled the binding of both salivary IgA1 and IgA2, with IgA2 predominating. For serum polyclonal IgA repertoire, substantially higher specificity was obtained. Serum IgA binding to E. coli correlated best with serum IgA binding to lipopolysaccharide (r = .86), and serum IgA against L. rhamnosus correlated best with the anti-peptidoglycan IgA levels (r = .88). We have also detected that total serum IgA response is governed by either IgA1 or IgA2 response, depending on the nature of the antigen/s. We conclude that steady state salivary IgA repertoire, unlike serum IgA repertoire, consists of polyreactive antibodies with innate specificity, questioning its capacity to select resident microbiota.",
publisher = "The Scandinavian Foundation for Immunology",
journal = "Scandinavian Journal of Immunology",
title = "Selectivity of polyclonal repertoire of anti-microbial IgA and its subclasses in saliva and serum in humans",
volume = "96",
doi = "10.1111/sji.13223"
}

Nikodijević, S., Blagojević, V., Ćuruvija, I., Kosanović, D., Đukić, T., Đorđević, B., Ilić, V.,& Minić, R.. (2022). Selectivity of polyclonal repertoire of anti-microbial IgA and its subclasses in saliva and serum in humans. in Scandinavian Journal of Immunology
The Scandinavian Foundation for Immunology., 96.
https://doi.org/10.1111/sji.13223

Nikodijević S, Blagojević V, Ćuruvija I, Kosanović D, Đukić T, Đorđević B, Ilić V, Minić R. Selectivity of polyclonal repertoire of anti-microbial IgA and its subclasses in saliva and serum in humans. in Scandinavian Journal of Immunology. 2022;96.
doi:10.1111/sji.13223 .

Nikodijević, Slavomir, Blagojević, Veljko, Ćuruvija, Ivana, Kosanović, Dejana, Đukić, Tamara, Đorđević, Brižita, Ilić, Vesna, Minić, Rajna, "Selectivity of polyclonal repertoire of anti-microbial IgA and its subclasses in saliva and serum in humans" in Scandinavian Journal of Immunology, 96 (2022),
https://doi.org/10.1111/sji.13223 . .

TY  - JOUR
AU  - Kosanović, Dejana
AU  - Dyas, Maria
AU  - Grogan, Helen
AU  - Kavanagh, Kevin
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/613
AB  - Trichoderma aggressivum, a mycopathogen causing green mould disease, is a major problem in Agaricus bisporus cultivation due to crop loss, and resistance to chemical fungicides. There is an urgent need for novel biological ways to control mycopathogens without affecting the growth of A. bisporus. Bacteria from the mushroom-casing environment were identified and tested for antagonistic effect on T. aggressivum. Bacillus velezensis produced a large zone of inhibition and its supernatant inhibited the growth of T. aggressivum [−37%], and slightly stimulated A. bisporus growth [+2%]. Label free quantitative-proteomic (LFQ) analysis of changes in the abundance of T. aggressivum proteins following exposure to B. velezensis supernatant indicated increased abundance of proteins associated with catabolic processing of amino acids (40-fold), amino oxidase proteins (14-fold), oxidoreductase proteins (13-fold, 4-fold) and hydrolases (3-fold). Proteins that decreased in relative abundance were antioxidants (29-fold), NTF2 domain containing protein (17-fold), 60S ribosomal protein L-13 (14-fold), glucoamylase proteins (13-fold), proteasome subunit proteins (11-fold) and other ribosomal proteins (9-fold). LFQ analysis revealed that exposing A. bisporus to B. velezensis supernatant led to a decrease in: prohibitin (13-fold, 6-fold), proteasomal proteins (11-fold), cytosolic adaptor domain containing protein (5-fold), aldehyde dehydrogenase (4-fold), ribosomal proteins (4-fold), DLH domain-containing protein (4-fold) and PKS_ER domain containing protein (3-fold). The results indicate that A. bisporus was not under stress upon contact with B. velezensis. Whereas a detrimental effect of B. velezensis on T. aggressivum is shown by inhibition of growth and damage-preventing proteins and increased abundance of proteins associated with stress.
PB  - Springer
T2  - European Journal of Plant Pathology
T1  - Differential proteomic response of Agaricus bisporus and Trichoderma aggressivum f. europaeum to Bacillus velezensis supernatant
IS  - 2
VL  - 160
VL  - 397
DO  - 10.1007/s10658-021-02252-5
ER  - 

@article{
author = "Kosanović, Dejana and Dyas, Maria and Grogan, Helen and Kavanagh, Kevin",
year = "2021",
abstract = "Trichoderma aggressivum, a mycopathogen causing green mould disease, is a major problem in Agaricus bisporus cultivation due to crop loss, and resistance to chemical fungicides. There is an urgent need for novel biological ways to control mycopathogens without affecting the growth of A. bisporus. Bacteria from the mushroom-casing environment were identified and tested for antagonistic effect on T. aggressivum. Bacillus velezensis produced a large zone of inhibition and its supernatant inhibited the growth of T. aggressivum [−37%], and slightly stimulated A. bisporus growth [+2%]. Label free quantitative-proteomic (LFQ) analysis of changes in the abundance of T. aggressivum proteins following exposure to B. velezensis supernatant indicated increased abundance of proteins associated with catabolic processing of amino acids (40-fold), amino oxidase proteins (14-fold), oxidoreductase proteins (13-fold, 4-fold) and hydrolases (3-fold). Proteins that decreased in relative abundance were antioxidants (29-fold), NTF2 domain containing protein (17-fold), 60S ribosomal protein L-13 (14-fold), glucoamylase proteins (13-fold), proteasome subunit proteins (11-fold) and other ribosomal proteins (9-fold). LFQ analysis revealed that exposing A. bisporus to B. velezensis supernatant led to a decrease in: prohibitin (13-fold, 6-fold), proteasomal proteins (11-fold), cytosolic adaptor domain containing protein (5-fold), aldehyde dehydrogenase (4-fold), ribosomal proteins (4-fold), DLH domain-containing protein (4-fold) and PKS_ER domain containing protein (3-fold). The results indicate that A. bisporus was not under stress upon contact with B. velezensis. Whereas a detrimental effect of B. velezensis on T. aggressivum is shown by inhibition of growth and damage-preventing proteins and increased abundance of proteins associated with stress.",
publisher = "Springer",
journal = "European Journal of Plant Pathology",
title = "Differential proteomic response of Agaricus bisporus and Trichoderma aggressivum f. europaeum to Bacillus velezensis supernatant",
number = "2",
volume = "160, 397",
doi = "10.1007/s10658-021-02252-5"
}

Kosanović, D., Dyas, M., Grogan, H.,& Kavanagh, K.. (2021). Differential proteomic response of Agaricus bisporus and Trichoderma aggressivum f. europaeum to Bacillus velezensis supernatant. in European Journal of Plant Pathology
Springer., 160(2).
https://doi.org/10.1007/s10658-021-02252-5

Kosanović D, Dyas M, Grogan H, Kavanagh K. Differential proteomic response of Agaricus bisporus and Trichoderma aggressivum f. europaeum to Bacillus velezensis supernatant. in European Journal of Plant Pathology. 2021;160(2).
doi:10.1007/s10658-021-02252-5 .

Kosanović, Dejana, Dyas, Maria, Grogan, Helen, Kavanagh, Kevin, "Differential proteomic response of Agaricus bisporus and Trichoderma aggressivum f. europaeum to Bacillus velezensis supernatant" in European Journal of Plant Pathology, 160, no. 2 (2021),
https://doi.org/10.1007/s10658-021-02252-5 . .