Dragačević, Luka

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orcid::0000-0003-1662-0493
  • Dragačević, Luka (13)
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Author's Bibliography

Supplementary information 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. Applied Biochemistry and Biotechnology 2022, 194, 2047–2060. https://doi.org/10.1007/s12010-021-03772-w.

Dragačević, Luka; Lopandić, Zorana; Gavrović-Jankulović, Marija; Živković, Irena; Blagojević, Veljko; Polović, Natalija; Minić, Rajna

(Springer, 2022)

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://intor.torlakinstitut.com/handle/123456789/642
AB  - SDS-PAGE showing: Lane 1 – purified banana lectin – BanLec; Lane 2 – chimera of banana lectin and enhanced green fluorescent protein BanLec-eGFP; Lane 3 – MW – molecular weight markers; Table 1. Repeatability of flow cytometric detection of different quantities of BL-eGFP binding to C. albicans; Table 2. Repeatability of ELLSA detection of different quantities of BanLec-B binding to C. albicans; Table 3. Repeatability of flow cytometric detection of different quantities of RCA120-FITC binding to L. casei DG; Table 4. Repeatability of ELLSA detection of different quantities of RCA120-B binding to L. casei DG; Table 5. Reproducibility of BanLec-B binding to 21 different microorganisms. Experiments were done in three different laboratories, with preparing new plates each time; Fig. 1 Determining linearity of ELLSA method, by measuring binding between C.albicans and different quantity of BanLec-B; Fig. 2 Determining linearity of flow cytometry, by measuring binding between C.albicans and different quantity of BanLec-eGFP; Fig. 3 Determining linearity of ELLSA method, by measuring binding between L.casei DG and different quantity of RCA120; Fig. 4 Determining linearity of flow cytometry, by measuring binding between L.casei DG and different quantity of RCA120.
PB  - Springer
T2  - Applied Biochemistry and Biotechnology
T1  - Supplementary information 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. Applied Biochemistry and Biotechnology 2022, 194, 2047–2060. https://doi.org/10.1007/s12010-021-03772-w.
EP  - 2060
SP  - 2047
VL  - 194
UR  - https://hdl.handle.net/21.15107/rcub_intor_642
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",
abstract = "SDS-PAGE showing: Lane 1 – purified banana lectin – BanLec; Lane 2 – chimera of banana lectin and enhanced green fluorescent protein BanLec-eGFP; Lane 3 – MW – molecular weight markers; Table 1. Repeatability of flow cytometric detection of different quantities of BL-eGFP binding to C. albicans; Table 2. Repeatability of ELLSA detection of different quantities of BanLec-B binding to C. albicans; Table 3. Repeatability of flow cytometric detection of different quantities of RCA120-FITC binding to L. casei DG; Table 4. Repeatability of ELLSA detection of different quantities of RCA120-B binding to L. casei DG; Table 5. Reproducibility of BanLec-B binding to 21 different microorganisms. Experiments were done in three different laboratories, with preparing new plates each time; Fig. 1 Determining linearity of ELLSA method, by measuring binding between C.albicans and different quantity of BanLec-B; Fig. 2 Determining linearity of flow cytometry, by measuring binding between C.albicans and different quantity of BanLec-eGFP; Fig. 3 Determining linearity of ELLSA method, by measuring binding between L.casei DG and different quantity of RCA120; Fig. 4 Determining linearity of flow cytometry, by measuring binding between L.casei DG and different quantity of RCA120.",
publisher = "Springer",
journal = "Applied Biochemistry and Biotechnology",
title = "Supplementary information 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. Applied Biochemistry and Biotechnology 2022, 194, 2047–2060. https://doi.org/10.1007/s12010-021-03772-w.",
pages = "2060-2047",
volume = "194",
url = "https://hdl.handle.net/21.15107/rcub_intor_642"
}
Dragačević, L., Lopandić, Z., Gavrović-Jankulović, M., Živković, I., Blagojević, V., Polović, N.,& Minić, R.. (2022). Supplementary information 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. Applied Biochemistry and Biotechnology 2022, 194, 2047–2060. https://doi.org/10.1007/s12010-021-03772-w.. in Applied Biochemistry and Biotechnology
Springer., 194, 2047-2060.
https://hdl.handle.net/21.15107/rcub_intor_642
Dragačević L, Lopandić Z, Gavrović-Jankulović M, Živković I, Blagojević V, Polović N, Minić R. Supplementary information 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. Applied Biochemistry and Biotechnology 2022, 194, 2047–2060. https://doi.org/10.1007/s12010-021-03772-w.. in Applied Biochemistry and Biotechnology. 2022;194:2047-2060.
https://hdl.handle.net/21.15107/rcub_intor_642 .
Dragačević, Luka, Lopandić, Zorana, Gavrović-Jankulović, Marija, Živković, Irena, Blagojević, Veljko, Polović, Natalija, Minić, Rajna, "Supplementary information 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. Applied Biochemistry and Biotechnology 2022, 194, 2047–2060. https://doi.org/10.1007/s12010-021-03772-w." in Applied Biochemistry and Biotechnology, 194 (2022):2047-2060,
https://hdl.handle.net/21.15107/rcub_intor_642 .

Differences in mouse strains determine the outcome of Der p 2 allergy induction protocols

Lopandić, Zorana; Dragačević, Luka; Kosanović, Dejana; Burazer, Lidija; Gavrović-Jankulović, Marija; Minić, Rajna

(Elsevier, 2022)

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 . .

Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1

Knežević, Sanja; Kosanović, Dejana; Dragačević, Luka; Živković, Irena; Ilić, Vesna; Hajduković, Ljiljana; Savić, Olivera; Minić, Rajna

(Elsevier, 2022)

TY  - JOUR
AU  - Knežević, Sanja
AU  - Kosanović, Dejana
AU  - Dragačević, Luka
AU  - Živković, Irena
AU  - Ilić, Vesna
AU  - Hajduković, Ljiljana
AU  - Savić, Olivera
AU  - Minić, Rajna
PY  - 2022
UR  - http://intor.torlakinstitut.com/handle/123456789/651
AB  - S. pneumoniae is an important human pathogen which has a polysaccharide capsule with virulent properties. This work aims to estimate the titres of S. pneumoniae specific IgG and IgA isotypes, with respect to age and sex. An in-house whole bacterial cell ELISA was used for the determination of relative levels and endpoint titres of IgG subclasses and IgA1 subclass specific for S. pneumoniae serogroup 1, and to quantify specific IgG1 and IgG2 levels. Significantly lower anti-pneumococcus IgG1 titres were found in older individuals, which was more pronounced in men. Lower IgG2 titres were detected in men over 50 years of age, in comparison to women under 50 years of age. The levels of IgG3 and IgG4 did not differ between different sex and age groups. Lower IgA1 levels were detected in male individuals in both age groups in comparison to females under 50 years of age. The levels of IgG1 showed a moderate correlation with IgG4 in younger individuals of both sexes (r = 0.61 in men and 0.63 in women) which was not noted in the older age group. We highlight the deficiency in humoral immunity in older people, especially male and suggest immunization of this population with pneumococcal vaccines.
PB  - Elsevier
T2  - Comparative Immunology, Microbiology and Infectious Diseases
T1  - Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1
SP  - 101834
VL  - 87
DO  - 10.1016/j.cimid.2022.101834
ER  - 
@article{
author = "Knežević, Sanja and Kosanović, Dejana and Dragačević, Luka and Živković, Irena and Ilić, Vesna and Hajduković, Ljiljana and Savić, Olivera and Minić, Rajna",
year = "2022",
abstract = "S. pneumoniae is an important human pathogen which has a polysaccharide capsule with virulent properties. This work aims to estimate the titres of S. pneumoniae specific IgG and IgA isotypes, with respect to age and sex. An in-house whole bacterial cell ELISA was used for the determination of relative levels and endpoint titres of IgG subclasses and IgA1 subclass specific for S. pneumoniae serogroup 1, and to quantify specific IgG1 and IgG2 levels. Significantly lower anti-pneumococcus IgG1 titres were found in older individuals, which was more pronounced in men. Lower IgG2 titres were detected in men over 50 years of age, in comparison to women under 50 years of age. The levels of IgG3 and IgG4 did not differ between different sex and age groups. Lower IgA1 levels were detected in male individuals in both age groups in comparison to females under 50 years of age. The levels of IgG1 showed a moderate correlation with IgG4 in younger individuals of both sexes (r = 0.61 in men and 0.63 in women) which was not noted in the older age group. We highlight the deficiency in humoral immunity in older people, especially male and suggest immunization of this population with pneumococcal vaccines.",
publisher = "Elsevier",
journal = "Comparative Immunology, Microbiology and Infectious Diseases",
title = "Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1",
pages = "101834",
volume = "87",
doi = "10.1016/j.cimid.2022.101834"
}
Knežević, S., Kosanović, D., Dragačević, L., Živković, I., Ilić, V., Hajduković, L., Savić, O.,& Minić, R.. (2022). Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1. in Comparative Immunology, Microbiology and Infectious Diseases
Elsevier., 87, 101834.
https://doi.org/10.1016/j.cimid.2022.101834
Knežević S, Kosanović D, Dragačević L, Živković I, Ilić V, Hajduković L, Savić O, Minić R. Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1. in Comparative Immunology, Microbiology and Infectious Diseases. 2022;87:101834.
doi:10.1016/j.cimid.2022.101834 .
Knežević, Sanja, Kosanović, Dejana, Dragačević, Luka, Živković, Irena, Ilić, Vesna, Hajduković, Ljiljana, Savić, Olivera, Minić, Rajna, "Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1" in Comparative Immunology, Microbiology and Infectious Diseases, 87 (2022):101834,
https://doi.org/10.1016/j.cimid.2022.101834 . .

Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1

Knežević, Sanja; Kosanović, Dejana; Dragačević, Luka; Živković, Irena; Ilić, Vesna; Hajduković, Ljiljana; Savić, Olivera; Minić, Rajna

(Elsevier, 2022)

TY  - JOUR
AU  - Knežević, Sanja
AU  - Kosanović, Dejana
AU  - Dragačević, Luka
AU  - Živković, Irena
AU  - Ilić, Vesna
AU  - Hajduković, Ljiljana
AU  - Savić, Olivera
AU  - Minić, Rajna
PY  - 2022
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/1255
UR  - http://intor.torlakinstitut.com/handle/123456789/650
AB  - S. pneumoniae is an important human pathogen which has a polysaccharide capsule with virulent properties. This work aims to estimate the titres of S. pneumoniae specific IgG and IgA isotypes, with respect to age and sex. An in-house whole bacterial cell ELISA was used for the determination of relative levels and endpoint titres of IgG subclasses and IgA1 subclass specific for S. pneumoniae serogroup 1, and to quantify specific IgG1 and IgG2 levels. Significantly lower anti-pneumococcus IgG1 titres were found in older individuals, which was more pronounced in men. Lower IgG2 titres were detected in men over 50 years of age, in comparison to women under 50 years of age. The levels of IgG3 and IgG4 did not differ between different sex and age groups. Lower IgA1 levels were detected in male individuals in both age groups in comparison to females under 50 years of age. The levels of IgG1 showed a moderate correlation with IgG4 in younger individuals of both sexes (r = 0.61 in men and 0.63 in women) which was not noted in the older age group. We highlight the deficiency in humoral immunity in older people, especially male and suggest immunization of this population with pneumococcal vaccines.
PB  - Elsevier
T2  - Comparative Immunology, Microbiology and Infectious Diseases
T1  - Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1
SP  - 101834
VL  - 87
DO  - 10.1016/j.cimid.2022.101834
ER  - 
@article{
author = "Knežević, Sanja and Kosanović, Dejana and Dragačević, Luka and Živković, Irena and Ilić, Vesna and Hajduković, Ljiljana and Savić, Olivera and Minić, Rajna",
year = "2022",
abstract = "S. pneumoniae is an important human pathogen which has a polysaccharide capsule with virulent properties. This work aims to estimate the titres of S. pneumoniae specific IgG and IgA isotypes, with respect to age and sex. An in-house whole bacterial cell ELISA was used for the determination of relative levels and endpoint titres of IgG subclasses and IgA1 subclass specific for S. pneumoniae serogroup 1, and to quantify specific IgG1 and IgG2 levels. Significantly lower anti-pneumococcus IgG1 titres were found in older individuals, which was more pronounced in men. Lower IgG2 titres were detected in men over 50 years of age, in comparison to women under 50 years of age. The levels of IgG3 and IgG4 did not differ between different sex and age groups. Lower IgA1 levels were detected in male individuals in both age groups in comparison to females under 50 years of age. The levels of IgG1 showed a moderate correlation with IgG4 in younger individuals of both sexes (r = 0.61 in men and 0.63 in women) which was not noted in the older age group. We highlight the deficiency in humoral immunity in older people, especially male and suggest immunization of this population with pneumococcal vaccines.",
publisher = "Elsevier",
journal = "Comparative Immunology, Microbiology and Infectious Diseases",
title = "Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1",
pages = "101834",
volume = "87",
doi = "10.1016/j.cimid.2022.101834"
}
Knežević, S., Kosanović, D., Dragačević, L., Živković, I., Ilić, V., Hajduković, L., Savić, O.,& Minić, R.. (2022). Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1. in Comparative Immunology, Microbiology and Infectious Diseases
Elsevier., 87, 101834.
https://doi.org/10.1016/j.cimid.2022.101834
Knežević S, Kosanović D, Dragačević L, Živković I, Ilić V, Hajduković L, Savić O, Minić R. Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1. in Comparative Immunology, Microbiology and Infectious Diseases. 2022;87:101834.
doi:10.1016/j.cimid.2022.101834 .
Knežević, Sanja, Kosanović, Dejana, Dragačević, Luka, Živković, Irena, Ilić, Vesna, Hajduković, Ljiljana, Savić, Olivera, Minić, Rajna, "Age and gender associated changes in immunoglobulin subclass levels specific to S. pneumoniae, serotype 1" in Comparative Immunology, Microbiology and Infectious Diseases, 87 (2022):101834,
https://doi.org/10.1016/j.cimid.2022.101834 . .

Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans

Dragačević, Luka; Lopandić, Zorana; Gavrović-Jankulović, Marija; Živković, Irena; Blagojević, Veljko; Polović, Natalija; Minić, Rajna

(Springer, 2022)

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://intor.torlakinstitut.com/handle/123456789/621
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
T1  - Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans
EP  - 2060
SP  - 2047
VL  - 194
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",
title = "Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans",
pages = "2060-2047",
volume = "194",
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 Profiling 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 Profiling 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 Profiling Microbial Glycans" in Applied Biochemistry and Biotechnology, 194 (2022):2047-2060,
https://doi.org/10.1007/s12010-021-03772-w . .
1
1

BCG vaccination induced alterations of thioglycollate-elicited peritoneal phagocytes: a case of trained immunity?

Ćuruvija, Ivana; Blagojević, Veljko; Dragačević, Luka; Vujić, Vesna; Lukić, Ivana; Stanojević, Stanislava

(Wiley, 2022)

TY  - JOUR
AU  - Ćuruvija, Ivana
AU  - Blagojević, Veljko
AU  - Dragačević, Luka
AU  - Vujić, Vesna
AU  - Lukić, Ivana
AU  - Stanojević, Stanislava
PY  - 2022
UR  - http://intor.torlakinstitut.com/handle/123456789/693
AB  - BCG vaccination induces a memory-like response in innate immune cells known as
trained immunity. In this study, we investigated the modification of innate immune
cells by BCG vaccination in acute peritoneal inflammation. We induced peritonitis with
thioglycollate (TG) in young Albino Oxford male rats which were immunised s.c. with
a BCG vaccine (BCG group) or saline (control group) 7 days prior. Peritoneal cells were
examined for 7 days after TG injection by flow cytometry, and for NO production and
peroxidase activity. Prior in vivo BCG priming altered TG-elicited peritoneal lavage
cells as following: increased in vitro LPS and BCG stimulated NO production from total
cells compared to adherent cells (day 1); increased cell number (days 3 and 5);
increased percentage of inflammatory monocytes (SSCmidCD43lowCD11bmid) and
eosinophils (SSCHihiS48+CD43hi), and a higher level of surface CD11b expression on
CD163+ macrophages (day 5); increased in vitro LPS and BCG stimulated peroxidase
activity (days 5 and 7); and increased percentage of CD163+MHCII+ cells (day 7). On
day 7, cells from both experimental groups showed no production of NO in response to
in vitro stimulation. We conclude that BCG vaccination had a substantial effect on the
acute phase of sterile inflammation, which may lead to the later observed phenotypic
and functional changes that could be seen as accelerated resolution of inflammation
and possibly point to trained immune response.
PB  - Wiley
T1  - BCG vaccination induced alterations of thioglycollate-elicited peritoneal phagocytes: a case of trained immunity?
EP  - 127
IS  - S2
SP  - 127
VL  - 52
UR  - https://hdl.handle.net/21.15107/rcub_intor_693
ER  - 
@article{
author = "Ćuruvija, Ivana and Blagojević, Veljko and Dragačević, Luka and Vujić, Vesna and Lukić, Ivana and Stanojević, Stanislava",
year = "2022",
abstract = "BCG vaccination induces a memory-like response in innate immune cells known as
trained immunity. In this study, we investigated the modification of innate immune
cells by BCG vaccination in acute peritoneal inflammation. We induced peritonitis with
thioglycollate (TG) in young Albino Oxford male rats which were immunised s.c. with
a BCG vaccine (BCG group) or saline (control group) 7 days prior. Peritoneal cells were
examined for 7 days after TG injection by flow cytometry, and for NO production and
peroxidase activity. Prior in vivo BCG priming altered TG-elicited peritoneal lavage
cells as following: increased in vitro LPS and BCG stimulated NO production from total
cells compared to adherent cells (day 1); increased cell number (days 3 and 5);
increased percentage of inflammatory monocytes (SSCmidCD43lowCD11bmid) and
eosinophils (SSCHihiS48+CD43hi), and a higher level of surface CD11b expression on
CD163+ macrophages (day 5); increased in vitro LPS and BCG stimulated peroxidase
activity (days 5 and 7); and increased percentage of CD163+MHCII+ cells (day 7). On
day 7, cells from both experimental groups showed no production of NO in response to
in vitro stimulation. We conclude that BCG vaccination had a substantial effect on the
acute phase of sterile inflammation, which may lead to the later observed phenotypic
and functional changes that could be seen as accelerated resolution of inflammation
and possibly point to trained immune response.",
publisher = "Wiley",
title = "BCG vaccination induced alterations of thioglycollate-elicited peritoneal phagocytes: a case of trained immunity?",
pages = "127-127",
number = "S2",
volume = "52",
url = "https://hdl.handle.net/21.15107/rcub_intor_693"
}
Ćuruvija, I., Blagojević, V., Dragačević, L., Vujić, V., Lukić, I.,& Stanojević, S.. (2022). BCG vaccination induced alterations of thioglycollate-elicited peritoneal phagocytes: a case of trained immunity?. 
Wiley., 52(S2), 127-127.
https://hdl.handle.net/21.15107/rcub_intor_693
Ćuruvija I, Blagojević V, Dragačević L, Vujić V, Lukić I, Stanojević S. BCG vaccination induced alterations of thioglycollate-elicited peritoneal phagocytes: a case of trained immunity?. 2022;52(S2):127-127.
https://hdl.handle.net/21.15107/rcub_intor_693 .
Ćuruvija, Ivana, Blagojević, Veljko, Dragačević, Luka, Vujić, Vesna, Lukić, Ivana, Stanojević, Stanislava, "BCG vaccination induced alterations of thioglycollate-elicited peritoneal phagocytes: a case of trained immunity?", 52, no. S2 (2022):127-127,
https://hdl.handle.net/21.15107/rcub_intor_693 .

Modifying Mycoplasma-infected lung immune cells through an intriguing interplay of BCG priming and peritoneal inflammation

Blagojević, Veljko; Ćuruvija, Ivana; Dragačević, Luka; Vujić, Vesna; Lukić, Ivana; Stanojević, Stanislava

(Wiley, 2022)

TY  - CONF
AU  - Blagojević, Veljko
AU  - Ćuruvija, Ivana
AU  - Dragačević, Luka
AU  - Vujić, Vesna
AU  - Lukić, Ivana
AU  - Stanojević, Stanislava
PY  - 2022
UR  - http://intor.torlakinstitut.com/handle/123456789/694
AB  - Inflammation is a redistribution of immune cells, providing a more efficient elimination of the inflammatory offense. However, it is not limited to local microenvironment. In this study, the interaction of the effect of BCG priming and peritoneal inflammation on the remote inflammatory milieu of infected lung was investigated. Young male AO rats infected with Mycoplasma spp. were s.c. injected with BCG (3x105 CFU) or saline, and 7 days later received an i.p. injection of 7ml of thioglycollate (TG) or saline. Up to 7 days after TG injection, a broncho-alveolar lavage (BAL) was performed, and cells were analysed for their surface marker expression and NO production. Infected rats had a high percentage of HIS48HiCD11bHi neutrophils. BCG priming didn’t alter BAL cells phenotype, while TG injection increased the proportion of MHCII+CD11blow activated alveolar macrophages (aAMFs) on day 7. However, the BCG+TG group showed significant changes – percentage of HIS48HiCD11bHi neutrophils decreased from day 3, the share of aAMFs increased from day 5 and the share of MHCII+CD11b-AMFs increased on days 3-5. However, the percentage of B220+FSClow B lymphocytes were increased from day 1. Production of NO from BAL fluid cells was low in all groups. We conclude that BCG vaccination likely increased the number of circulating B lymphocytes, while TG-induced peritoneal inflammation potentially prevented their entry into the peritoneal cavity, forcing them into permissive tissues, such as lungs.
PB  - Wiley
T1  - Modifying Mycoplasma-infected lung immune cells through an intriguing interplay of BCG priming and peritoneal inflammation
EP  - 55
IS  - S2
SP  - 55
VL  - 52
UR  - https://hdl.handle.net/21.15107/rcub_intor_694
ER  - 
@conference{
author = "Blagojević, Veljko and Ćuruvija, Ivana and Dragačević, Luka and Vujić, Vesna and Lukić, Ivana and Stanojević, Stanislava",
year = "2022",
abstract = "Inflammation is a redistribution of immune cells, providing a more efficient elimination of the inflammatory offense. However, it is not limited to local microenvironment. In this study, the interaction of the effect of BCG priming and peritoneal inflammation on the remote inflammatory milieu of infected lung was investigated. Young male AO rats infected with Mycoplasma spp. were s.c. injected with BCG (3x105 CFU) or saline, and 7 days later received an i.p. injection of 7ml of thioglycollate (TG) or saline. Up to 7 days after TG injection, a broncho-alveolar lavage (BAL) was performed, and cells were analysed for their surface marker expression and NO production. Infected rats had a high percentage of HIS48HiCD11bHi neutrophils. BCG priming didn’t alter BAL cells phenotype, while TG injection increased the proportion of MHCII+CD11blow activated alveolar macrophages (aAMFs) on day 7. However, the BCG+TG group showed significant changes – percentage of HIS48HiCD11bHi neutrophils decreased from day 3, the share of aAMFs increased from day 5 and the share of MHCII+CD11b-AMFs increased on days 3-5. However, the percentage of B220+FSClow B lymphocytes were increased from day 1. Production of NO from BAL fluid cells was low in all groups. We conclude that BCG vaccination likely increased the number of circulating B lymphocytes, while TG-induced peritoneal inflammation potentially prevented their entry into the peritoneal cavity, forcing them into permissive tissues, such as lungs.",
publisher = "Wiley",
title = "Modifying Mycoplasma-infected lung immune cells through an intriguing interplay of BCG priming and peritoneal inflammation",
pages = "55-55",
number = "S2",
volume = "52",
url = "https://hdl.handle.net/21.15107/rcub_intor_694"
}
Blagojević, V., Ćuruvija, I., Dragačević, L., Vujić, V., Lukić, I.,& Stanojević, S.. (2022). Modifying Mycoplasma-infected lung immune cells through an intriguing interplay of BCG priming and peritoneal inflammation. 
Wiley., 52(S2), 55-55.
https://hdl.handle.net/21.15107/rcub_intor_694
Blagojević V, Ćuruvija I, Dragačević L, Vujić V, Lukić I, Stanojević S. Modifying Mycoplasma-infected lung immune cells through an intriguing interplay of BCG priming and peritoneal inflammation. 2022;52(S2):55-55.
https://hdl.handle.net/21.15107/rcub_intor_694 .
Blagojević, Veljko, Ćuruvija, Ivana, Dragačević, Luka, Vujić, Vesna, Lukić, Ivana, Stanojević, Stanislava, "Modifying Mycoplasma-infected lung immune cells through an intriguing interplay of BCG priming and peritoneal inflammation", 52, no. S2 (2022):55-55,
https://hdl.handle.net/21.15107/rcub_intor_694 .

BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms

Lopandic, Zorana; Dragačević, Luka; Popovic, Dragan; Andjelkovic, Uros; Minić, Rajna; Gavrovic-Jankulovic, Marija

(MDPI, 2021)

TY  - JOUR
AU  - Lopandic, Zorana
AU  - Dragačević, Luka
AU  - Popovic, Dragan
AU  - Andjelkovic, Uros
AU  - Minić, Rajna
AU  - Gavrovic-Jankulovic, Marija
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/615
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
T1  - BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms
IS  - 2
SP  - 180
VL  - 11(2)
VL  - 11
DO  - 10.3390/biom11020180
ER  - 
@article{
author = "Lopandic, Zorana and Dragačević, Luka and Popovic, Dragan and Andjelkovic, Uros and Minić, Rajna and Gavrovic-Jankulovic, 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",
title = "BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms",
number = "2",
pages = "180",
volume = "11(2), 11",
doi = "10.3390/biom11020180"
}
Lopandic, Z., Dragačević, L., Popovic, D., Andjelkovic, U., Minić, R.,& Gavrovic-Jankulovic, M.. (2021). BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms. in Biomolecules
MDPI., 11(2)(2), 180.
https://doi.org/10.3390/biom11020180
Lopandic Z, Dragačević L, Popovic D, Andjelkovic U, Minić R, Gavrovic-Jankulovic M. BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms. in Biomolecules. 2021;11(2)(2):180.
doi:10.3390/biom11020180 .
Lopandic, Zorana, Dragačević, Luka, Popovic, Dragan, Andjelkovic, Uros, Minić, Rajna, Gavrovic-Jankulovic, Marija, "BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms" in Biomolecules, 11(2), no. 2 (2021):180,
https://doi.org/10.3390/biom11020180 . .
7
2
8

ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin

Dragačević, Luka; Đorđević, Brižita; Gavrović-Jankulović, Marija; Ilić, Vesna; Kanazir, Danijela; Minić, Rajna

(Springer, Dordrecht, 2020)

TY  - JOUR
AU  - Dragačević, Luka
AU  - Đorđević, Brižita
AU  - Gavrović-Jankulović, Marija
AU  - Ilić, Vesna
AU  - Kanazir, Danijela
AU  - Minić, Rajna
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/653
AB  - The surface of microorganisms is covered with polysaccharide structures which are in immediate contact with receptor structures on host's cells and antibodies. The interaction between microorganisms and their host is dependent on surface glycosylation and in this study we have tested the interaction of plant lectins with different microorganisms. Enzyme-linked lectin sorbent assay - ELLSA was used to test the binding of recombinant Musa acuminata lectin - BL to 27 selected microorganisms and 7 other lectins were used for comparison: Soy bean agglutinin - SBA, Lens culinaris lectin - LCA, Wheat germ agglutinin - WGA, RCA(120) - Ricinus communis agglutinin, Con A - from Canavalia ensiformis, Sambucus nigra agglutinin - SNA I and Maackia amurensis agglutinin - MAA. The goal was to define the microorganisms' surface glycosylation by means of interaction with the selected plant lectins and to make a comparison with BL. Among the tested lectins most selective binding was observed for RCA(120) which preferentially bound Lactobacillus casei DG. Recombinant banana lectin showed specific binding to all of the tested fungal species. The binding of BL to Candida albicans was further tested with fluorescence microscopy and flow cytometry and it was concluded that this lectin can differentiate ss-glucan rich surfaces. The binding of BL to S. boulardii could be inhibited with ss-glucan from yeast with IC50 1.81 mu g mL(-1) and to P. roqueforti with 1.10 mu g mL(-1). This unique specificity of BL could be exploited for screening purposes and potentially for the detection of ss-glucan in solutions.
PB  - Springer, Dordrecht
T2  - Glycoconjugate Journal
T1  - ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin
EP  - 105
IS  - 1
SP  - 95
VL  - 37
DO  - 10.1007/s10719-019-09898-8
ER  - 
@article{
author = "Dragačević, Luka and Đorđević, Brižita and Gavrović-Jankulović, Marija and Ilić, Vesna and Kanazir, Danijela and Minić, Rajna",
year = "2020",
abstract = "The surface of microorganisms is covered with polysaccharide structures which are in immediate contact with receptor structures on host's cells and antibodies. The interaction between microorganisms and their host is dependent on surface glycosylation and in this study we have tested the interaction of plant lectins with different microorganisms. Enzyme-linked lectin sorbent assay - ELLSA was used to test the binding of recombinant Musa acuminata lectin - BL to 27 selected microorganisms and 7 other lectins were used for comparison: Soy bean agglutinin - SBA, Lens culinaris lectin - LCA, Wheat germ agglutinin - WGA, RCA(120) - Ricinus communis agglutinin, Con A - from Canavalia ensiformis, Sambucus nigra agglutinin - SNA I and Maackia amurensis agglutinin - MAA. The goal was to define the microorganisms' surface glycosylation by means of interaction with the selected plant lectins and to make a comparison with BL. Among the tested lectins most selective binding was observed for RCA(120) which preferentially bound Lactobacillus casei DG. Recombinant banana lectin showed specific binding to all of the tested fungal species. The binding of BL to Candida albicans was further tested with fluorescence microscopy and flow cytometry and it was concluded that this lectin can differentiate ss-glucan rich surfaces. The binding of BL to S. boulardii could be inhibited with ss-glucan from yeast with IC50 1.81 mu g mL(-1) and to P. roqueforti with 1.10 mu g mL(-1). This unique specificity of BL could be exploited for screening purposes and potentially for the detection of ss-glucan in solutions.",
publisher = "Springer, Dordrecht",
journal = "Glycoconjugate Journal",
title = "ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin",
pages = "105-95",
number = "1",
volume = "37",
doi = "10.1007/s10719-019-09898-8"
}
Dragačević, L., Đorđević, B., Gavrović-Jankulović, M., Ilić, V., Kanazir, D.,& Minić, R.. (2020). ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin. in Glycoconjugate Journal
Springer, Dordrecht., 37(1), 95-105.
https://doi.org/10.1007/s10719-019-09898-8
Dragačević L, Đorđević B, Gavrović-Jankulović M, Ilić V, Kanazir D, Minić R. ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin. in Glycoconjugate Journal. 2020;37(1):95-105.
doi:10.1007/s10719-019-09898-8 .
Dragačević, Luka, Đorđević, Brižita, Gavrović-Jankulović, Marija, Ilić, Vesna, Kanazir, Danijela, Minić, Rajna, "ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin" in Glycoconjugate Journal, 37, no. 1 (2020):95-105,
https://doi.org/10.1007/s10719-019-09898-8 . .
2
7
3
5

Comparison of Specific IGG and IGA Subclass Levels to Lactobacillus and Streptococcus in Young Healthy Adults

Dragačević, Luka; Minić, Rajna; Michalickova, Danica; Ilić, Vesna; Đorđević, Brižita

(Lippincott Williams & Wilkins, Philadelphia, 2020)

TY  - CONF
AU  - Dragačević, Luka
AU  - Minić, Rajna
AU  - Michalickova, Danica
AU  - Ilić, Vesna
AU  - Đorđević, Brižita
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/568
PB  - Lippincott Williams & Wilkins, Philadelphia
C3  - Journal of Clinical Gastroenterology
T1  - Comparison of Specific IGG and IGA Subclass Levels to Lactobacillus and Streptococcus in Young Healthy Adults
EP  - S18
SP  - S18
VL  - 54
UR  - https://hdl.handle.net/21.15107/rcub_intor_568
ER  - 
@conference{
author = "Dragačević, Luka and Minić, Rajna and Michalickova, Danica and Ilić, Vesna and Đorđević, Brižita",
year = "2020",
publisher = "Lippincott Williams & Wilkins, Philadelphia",
journal = "Journal of Clinical Gastroenterology",
title = "Comparison of Specific IGG and IGA Subclass Levels to Lactobacillus and Streptococcus in Young Healthy Adults",
pages = "S18-S18",
volume = "54",
url = "https://hdl.handle.net/21.15107/rcub_intor_568"
}
Dragačević, L., Minić, R., Michalickova, D., Ilić, V.,& Đorđević, B.. (2020). Comparison of Specific IGG and IGA Subclass Levels to Lactobacillus and Streptococcus in Young Healthy Adults. in Journal of Clinical Gastroenterology
Lippincott Williams & Wilkins, Philadelphia., 54, S18-S18.
https://hdl.handle.net/21.15107/rcub_intor_568
Dragačević L, Minić R, Michalickova D, Ilić V, Đorđević B. Comparison of Specific IGG and IGA Subclass Levels to Lactobacillus and Streptococcus in Young Healthy Adults. in Journal of Clinical Gastroenterology. 2020;54:S18-S18.
https://hdl.handle.net/21.15107/rcub_intor_568 .
Dragačević, Luka, Minić, Rajna, Michalickova, Danica, Ilić, Vesna, Đorđević, Brižita, "Comparison of Specific IGG and IGA Subclass Levels to Lactobacillus and Streptococcus in Young Healthy Adults" in Journal of Clinical Gastroenterology, 54 (2020):S18-S18,
https://hdl.handle.net/21.15107/rcub_intor_568 .

Typing of Surface Glycosilation of Microorganisms by Lectins with in House Elisa

Dragačević, Luka; Đorđević, Brižita; Gavrović-Jankulović, Marija; Ilić, Vesna; Minić, Rajna

(Lippincott Williams & Wilkins, Philadelphia, 2020)

TY  - CONF
AU  - Dragačević, Luka
AU  - Đorđević, Brižita
AU  - Gavrović-Jankulović, Marija
AU  - Ilić, Vesna
AU  - Minić, Rajna
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/567
PB  - Lippincott Williams & Wilkins, Philadelphia
C3  - Journal of Clinical Gastroenterology
T1  - Typing of Surface Glycosilation of Microorganisms by Lectins with in House Elisa
EP  - S13
SP  - S13
VL  - 54
UR  - https://hdl.handle.net/21.15107/rcub_intor_567
ER  - 
@conference{
author = "Dragačević, Luka and Đorđević, Brižita and Gavrović-Jankulović, Marija and Ilić, Vesna and Minić, Rajna",
year = "2020",
publisher = "Lippincott Williams & Wilkins, Philadelphia",
journal = "Journal of Clinical Gastroenterology",
title = "Typing of Surface Glycosilation of Microorganisms by Lectins with in House Elisa",
pages = "S13-S13",
volume = "54",
url = "https://hdl.handle.net/21.15107/rcub_intor_567"
}
Dragačević, L., Đorđević, B., Gavrović-Jankulović, M., Ilić, V.,& Minić, R.. (2020). Typing of Surface Glycosilation of Microorganisms by Lectins with in House Elisa. in Journal of Clinical Gastroenterology
Lippincott Williams & Wilkins, Philadelphia., 54, S13-S13.
https://hdl.handle.net/21.15107/rcub_intor_567
Dragačević L, Đorđević B, Gavrović-Jankulović M, Ilić V, Minić R. Typing of Surface Glycosilation of Microorganisms by Lectins with in House Elisa. in Journal of Clinical Gastroenterology. 2020;54:S13-S13.
https://hdl.handle.net/21.15107/rcub_intor_567 .
Dragačević, Luka, Đorđević, Brižita, Gavrović-Jankulović, Marija, Ilić, Vesna, Minić, Rajna, "Typing of Surface Glycosilation of Microorganisms by Lectins with in House Elisa" in Journal of Clinical Gastroenterology, 54 (2020):S13-S13,
https://hdl.handle.net/21.15107/rcub_intor_567 .

ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin

Dragačević, Luka; Đorđević, Brižita; Gavrović-Jankulović, Marija; Ilić, Vesna; Kanazir, Danijela; Minić, Rajna

(Springer, Dordrecht, 2020)

TY  - JOUR
AU  - Dragačević, Luka
AU  - Đorđević, Brižita
AU  - Gavrović-Jankulović, Marija
AU  - Ilić, Vesna
AU  - Kanazir, Danijela
AU  - Minić, Rajna
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/563
AB  - The surface of microorganisms is covered with polysaccharide structures which are in immediate contact with receptor structures on host's cells and antibodies. The interaction between microorganisms and their host is dependent on surface glycosylation and in this study we have tested the interaction of plant lectins with different microorganisms. Enzyme-linked lectin sorbent assay - ELLSA was used to test the binding of recombinant Musa acuminata lectin - BL to 27 selected microorganisms and 7 other lectins were used for comparison: Soy bean agglutinin - SBA, Lens culinaris lectin - LCA, Wheat germ agglutinin - WGA, RCA(120) - Ricinus communis agglutinin, Con A - from Canavalia ensiformis, Sambucus nigra agglutinin - SNA I and Maackia amurensis agglutinin - MAA. The goal was to define the microorganisms' surface glycosylation by means of interaction with the selected plant lectins and to make a comparison with BL. Among the tested lectins most selective binding was observed for RCA(120) which preferentially bound Lactobacillus casei DG. Recombinant banana lectin showed specific binding to all of the tested fungal species. The binding of BL to Candida albicans was further tested with fluorescence microscopy and flow cytometry and it was concluded that this lectin can differentiate ss-glucan rich surfaces. The binding of BL to S. boulardii could be inhibited with ss-glucan from yeast with IC50 1.81 mu g mL(-1) and to P. roqueforti with 1.10 mu g mL(-1). This unique specificity of BL could be exploited for screening purposes and potentially for the detection of ss-glucan in solutions.
PB  - Springer, Dordrecht
T2  - Glycoconjugate Journal
T1  - ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin
EP  - 105
IS  - 1
SP  - 95
VL  - 37
DO  - 10.1007/s10719-019-09898-8
ER  - 
@article{
author = "Dragačević, Luka and Đorđević, Brižita and Gavrović-Jankulović, Marija and Ilić, Vesna and Kanazir, Danijela and Minić, Rajna",
year = "2020",
abstract = "The surface of microorganisms is covered with polysaccharide structures which are in immediate contact with receptor structures on host's cells and antibodies. The interaction between microorganisms and their host is dependent on surface glycosylation and in this study we have tested the interaction of plant lectins with different microorganisms. Enzyme-linked lectin sorbent assay - ELLSA was used to test the binding of recombinant Musa acuminata lectin - BL to 27 selected microorganisms and 7 other lectins were used for comparison: Soy bean agglutinin - SBA, Lens culinaris lectin - LCA, Wheat germ agglutinin - WGA, RCA(120) - Ricinus communis agglutinin, Con A - from Canavalia ensiformis, Sambucus nigra agglutinin - SNA I and Maackia amurensis agglutinin - MAA. The goal was to define the microorganisms' surface glycosylation by means of interaction with the selected plant lectins and to make a comparison with BL. Among the tested lectins most selective binding was observed for RCA(120) which preferentially bound Lactobacillus casei DG. Recombinant banana lectin showed specific binding to all of the tested fungal species. The binding of BL to Candida albicans was further tested with fluorescence microscopy and flow cytometry and it was concluded that this lectin can differentiate ss-glucan rich surfaces. The binding of BL to S. boulardii could be inhibited with ss-glucan from yeast with IC50 1.81 mu g mL(-1) and to P. roqueforti with 1.10 mu g mL(-1). This unique specificity of BL could be exploited for screening purposes and potentially for the detection of ss-glucan in solutions.",
publisher = "Springer, Dordrecht",
journal = "Glycoconjugate Journal",
title = "ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin",
pages = "105-95",
number = "1",
volume = "37",
doi = "10.1007/s10719-019-09898-8"
}
Dragačević, L., Đorđević, B., Gavrović-Jankulović, M., Ilić, V., Kanazir, D.,& Minić, R.. (2020). ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin. in Glycoconjugate Journal
Springer, Dordrecht., 37(1), 95-105.
https://doi.org/10.1007/s10719-019-09898-8
Dragačević L, Đorđević B, Gavrović-Jankulović M, Ilić V, Kanazir D, Minić R. ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin. in Glycoconjugate Journal. 2020;37(1):95-105.
doi:10.1007/s10719-019-09898-8 .
Dragačević, Luka, Đorđević, Brižita, Gavrović-Jankulović, Marija, Ilić, Vesna, Kanazir, Danijela, Minić, Rajna, "ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin" in Glycoconjugate Journal, 37, no. 1 (2020):95-105,
https://doi.org/10.1007/s10719-019-09898-8 . .
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Direct UV Spectrophotometry and HPLC Determination of Triton X-100 in Split Virus Influenza Vaccine

Pavlović, Bojana; Cvijetić, Nataša; Dragačević, Luka; Ivković, Branka; Vujić, Zorica; Kuntić, Vesna

(Oxford Univ Press Inc, Cary, 2016)

TY  - JOUR
AU  - Pavlović, Bojana
AU  - Cvijetić, Nataša
AU  - Dragačević, Luka
AU  - Ivković, Branka
AU  - Vujić, Zorica
AU  - Kuntić, Vesna
PY  - 2016
UR  - http://intor.torlakinstitut.com/handle/123456789/469
AB  - One of the most commonly used surfactants in the production of split virus influenza vaccine is nonionic surfactant Triton X-100. After splitting of the virus is accomplished, Triton X-100 is removed from the vaccine by subsequent production steps. Because of toxicity of Triton X-100, which remains in the vaccine in residual amounts, a sufficiently sensitive method for its detection and quantification needs to be defined. Two methods for determination of Triton X-100 residuals were developed: the UV-spectrophotometry and HPLC methods. For both methods, preparation of vaccine samples and removal of proteins and virus particles were crucial: samples were treated with methanol (1:1) and then centrifuged at 25000 x g for 30 min. After such treatment, the majority of vaccine components that interfered in the UV region were removed, and diluted samples could be directly measured. The chromatographic system included C18 column, step methanol gradient, and detection at 225 nm with a single peak of Triton X-100 at 12.6 min. Both methods were validated and gave satisfactory results for accuracy, precision, specificity, linearity, and robustness. LOQ was slightly lower for the HPLC method. Hence, it was shown that both methods are suitable for analysis of residual amounts of Triton X-100, with the advantages of the UV method being its simplicity and availability in most laboratories.
PB  - Oxford Univ Press Inc, Cary
T2  - Journal of AOAC International
T1  - Direct UV Spectrophotometry and HPLC Determination of Triton X-100 in Split Virus Influenza Vaccine
EP  - 400
IS  - 2
SP  - 396
VL  - 99
DO  - 10.5740/jaoacint.15-0201
ER  - 
@article{
author = "Pavlović, Bojana and Cvijetić, Nataša and Dragačević, Luka and Ivković, Branka and Vujić, Zorica and Kuntić, Vesna",
year = "2016",
abstract = "One of the most commonly used surfactants in the production of split virus influenza vaccine is nonionic surfactant Triton X-100. After splitting of the virus is accomplished, Triton X-100 is removed from the vaccine by subsequent production steps. Because of toxicity of Triton X-100, which remains in the vaccine in residual amounts, a sufficiently sensitive method for its detection and quantification needs to be defined. Two methods for determination of Triton X-100 residuals were developed: the UV-spectrophotometry and HPLC methods. For both methods, preparation of vaccine samples and removal of proteins and virus particles were crucial: samples were treated with methanol (1:1) and then centrifuged at 25000 x g for 30 min. After such treatment, the majority of vaccine components that interfered in the UV region were removed, and diluted samples could be directly measured. The chromatographic system included C18 column, step methanol gradient, and detection at 225 nm with a single peak of Triton X-100 at 12.6 min. Both methods were validated and gave satisfactory results for accuracy, precision, specificity, linearity, and robustness. LOQ was slightly lower for the HPLC method. Hence, it was shown that both methods are suitable for analysis of residual amounts of Triton X-100, with the advantages of the UV method being its simplicity and availability in most laboratories.",
publisher = "Oxford Univ Press Inc, Cary",
journal = "Journal of AOAC International",
title = "Direct UV Spectrophotometry and HPLC Determination of Triton X-100 in Split Virus Influenza Vaccine",
pages = "400-396",
number = "2",
volume = "99",
doi = "10.5740/jaoacint.15-0201"
}
Pavlović, B., Cvijetić, N., Dragačević, L., Ivković, B., Vujić, Z.,& Kuntić, V.. (2016). Direct UV Spectrophotometry and HPLC Determination of Triton X-100 in Split Virus Influenza Vaccine. in Journal of AOAC International
Oxford Univ Press Inc, Cary., 99(2), 396-400.
https://doi.org/10.5740/jaoacint.15-0201
Pavlović B, Cvijetić N, Dragačević L, Ivković B, Vujić Z, Kuntić V. Direct UV Spectrophotometry and HPLC Determination of Triton X-100 in Split Virus Influenza Vaccine. in Journal of AOAC International. 2016;99(2):396-400.
doi:10.5740/jaoacint.15-0201 .
Pavlović, Bojana, Cvijetić, Nataša, Dragačević, Luka, Ivković, Branka, Vujić, Zorica, Kuntić, Vesna, "Direct UV Spectrophotometry and HPLC Determination of Triton X-100 in Split Virus Influenza Vaccine" in Journal of AOAC International, 99, no. 2 (2016):396-400,
https://doi.org/10.5740/jaoacint.15-0201 . .
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