Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry)

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Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry) (en)
Ministarstvo prosvete, nauke i tehnološkog razvoja Republike Srbije, Ugovor br. 451-03-68/2020-14/200168 (Univerzitet u Beogradu, Hemijski fakultet) (sr_RS)
Министарство просвете, науке и технолошког развоја Републике Србије, Уговор бр. 451-03-68/2020-14/200168 (Универзитет у Београду, Хемијски факултет) (sr)
Authors

Publications

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

Lopandic, Zorana; Dragacevic, Luka; Popovic, Dragan; Andjelkovic, Uros; Minic, Rajna; Gavrovic-Jankulovic, Marija

(MDPI, 2021)

TY  - JOUR
AU  - Lopandic, Zorana
AU  - Dragacevic, Luka
AU  - Popovic, Dragan
AU  - Andjelkovic, Uros
AU  - Minic, 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 Dragacevic, Luka and Popovic, Dragan and Andjelkovic, Uros and Minic, 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., Dragacevic, L., Popovic, D., Andjelkovic, U., Minic, 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, Dragacevic L, Popovic D, Andjelkovic U, Minic 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, Dragacevic, Luka, Popovic, Dragan, Andjelkovic, Uros, Minic, 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 . .
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Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia

Stojanović, Marijana; Lukić, Ivana; Marinković, Emilija; Kovačević, Ana; Miljković, Radmila; Tobias, Joshua; Schabussova, Irma; Zlatović, Mario; Barisani-Asenbauer, Talin; Wiedermann, Ursula; Inić-Kanada, Aleksandra

(MDPI, Basel, 2020)

TY  - JOUR
AU  - Stojanović, Marijana
AU  - Lukić, Ivana
AU  - Marinković, Emilija
AU  - Kovačević, Ana
AU  - Miljković, Radmila
AU  - Tobias, Joshua
AU  - Schabussova, Irma
AU  - Zlatović, Mario
AU  - Barisani-Asenbauer, Talin
AU  - Wiedermann, Ursula
AU  - Inić-Kanada, Aleksandra
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/552
AB  - Vaccines can have heterologous effects on the immune system, i.e., effects other than triggering an immune response against the disease targeted by the vaccine. We investigated whether monoclonal antibodies (mAbs) specific for tetanus could cross-react with Chlamydia and confer heterologous protection against chlamydial infection. The capability of two tetanus-specific mAbs, namely mAb26 and mAb51, to prevent chlamydial infection has been assessed: (i) in vitro, by performing a neutralization assay using human conjunctival epithelial (HCjE) cells infected with Chlamydia trachomatis serovar B, and (ii) in vivo, by using a guinea pig model of Chlamydia caviae-induced inclusion conjunctivitis. The mAb26 has been superior in comparison with mAb51 in the prevention of chlamydial infection in HCjE cells. The mAb26 has conferred approximate to 40% inhibition of the infection, compared to less than 5% inhibition in the presence of the mAb51. In vivo, mAb26 significantly diminished ocular pathology intensity in guinea pigs infected with C. caviae compared to either the mAb51-treated or sham-treated guinea pigs. Our data provide insights that tetanus immunization generates antibodies which induce heterologous chlamydial immunity and promote protection beyond the intended target pathogen.
PB  - MDPI, Basel
T2  - Vaccines
T1  - Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia
IS  - 4
SP  - 719
VL  - 8
DO  - 10.3390/vaccines8040719
UR  - conv_488
ER  - 
@article{
author = "Stojanović, Marijana and Lukić, Ivana and Marinković, Emilija and Kovačević, Ana and Miljković, Radmila and Tobias, Joshua and Schabussova, Irma and Zlatović, Mario and Barisani-Asenbauer, Talin and Wiedermann, Ursula and Inić-Kanada, Aleksandra",
year = "2020",
abstract = "Vaccines can have heterologous effects on the immune system, i.e., effects other than triggering an immune response against the disease targeted by the vaccine. We investigated whether monoclonal antibodies (mAbs) specific for tetanus could cross-react with Chlamydia and confer heterologous protection against chlamydial infection. The capability of two tetanus-specific mAbs, namely mAb26 and mAb51, to prevent chlamydial infection has been assessed: (i) in vitro, by performing a neutralization assay using human conjunctival epithelial (HCjE) cells infected with Chlamydia trachomatis serovar B, and (ii) in vivo, by using a guinea pig model of Chlamydia caviae-induced inclusion conjunctivitis. The mAb26 has been superior in comparison with mAb51 in the prevention of chlamydial infection in HCjE cells. The mAb26 has conferred approximate to 40% inhibition of the infection, compared to less than 5% inhibition in the presence of the mAb51. In vivo, mAb26 significantly diminished ocular pathology intensity in guinea pigs infected with C. caviae compared to either the mAb51-treated or sham-treated guinea pigs. Our data provide insights that tetanus immunization generates antibodies which induce heterologous chlamydial immunity and promote protection beyond the intended target pathogen.",
publisher = "MDPI, Basel",
journal = "Vaccines",
title = "Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia",
number = "4",
pages = "719",
volume = "8",
doi = "10.3390/vaccines8040719",
url = "conv_488"
}
Stojanović, M., Lukić, I., Marinković, E., Kovačević, A., Miljković, R., Tobias, J., Schabussova, I., Zlatović, M., Barisani-Asenbauer, T., Wiedermann, U.,& Inić-Kanada, A.. (2020). Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia. in Vaccines
MDPI, Basel., 8(4), 719.
https://doi.org/10.3390/vaccines8040719
conv_488
Stojanović M, Lukić I, Marinković E, Kovačević A, Miljković R, Tobias J, Schabussova I, Zlatović M, Barisani-Asenbauer T, Wiedermann U, Inić-Kanada A. Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia. in Vaccines. 2020;8(4):719.
doi:10.3390/vaccines8040719
conv_488 .
Stojanović, Marijana, Lukić, Ivana, Marinković, Emilija, Kovačević, Ana, Miljković, Radmila, Tobias, Joshua, Schabussova, Irma, Zlatović, Mario, Barisani-Asenbauer, Talin, Wiedermann, Ursula, Inić-Kanada, Aleksandra, "Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia" in Vaccines, 8, no. 4 (2020):719,
https://doi.org/10.3390/vaccines8040719 .,
conv_488 .
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Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation

Radosavljević, Jelena; Apostolović, Danijela; Mihailović, Jelena; Atanasković-Marković, Marina; Burazer, Lidija; van Hage, Marianne; Ćirković-Veličković, Tanja

(MDPI, Basel, 2020)

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/547
AB  - The aim of this study was to identify short digestion-resistant peptides (SDRPs) released by pepsin digestion of the whole cow's milk and examine their IgE reactivity and allergenicity. Raw milk was subjected to simulated gastric digestion. SDRPs were fractionated from the digests and identified by MS. Milk SDRPs were evaluated for aggregability, propensity to compete for IgE binding with individual milk allergens, and ability to bind IgG4 from allergic and milk-tolerant individuals. The majority of milk SDRPs originated from caseins (97% of peptides) and overlapped with the known IgE epitopes of cow's milk allergens. SDRPs competed with milk proteins for binding to human IgE and readily formed aggregates. The average peptide length was 10.6 +/- 3.5 amino acids. The ability to provoke allergenic in vivo responses was confirmed by skin-prick testing (SPT) in five milk-allergic subjects. This was attributed to the peptide ability to aggregate into non-covalent complexes. SDRPs are able to induce response in SPT, but only in 50% of the sera SDRPs were able to inhibit IgG4 binding to caseins. Hence, SDRPs corresponding to the mainly continuous epitopes of milk proteins induce allergenic in vivo responses in milk-allergic subjects due to aggregation.
PB  - MDPI, Basel
T2  - Foods
T1  - Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation
IS  - 11
VL  - 9
DO  - 10.3390/foods9111576
UR  - conv_485
ER  - 
@article{
author = "Radosavljević, Jelena and Apostolović, Danijela and Mihailović, Jelena and Atanasković-Marković, Marina and Burazer, Lidija and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "The aim of this study was to identify short digestion-resistant peptides (SDRPs) released by pepsin digestion of the whole cow's milk and examine their IgE reactivity and allergenicity. Raw milk was subjected to simulated gastric digestion. SDRPs were fractionated from the digests and identified by MS. Milk SDRPs were evaluated for aggregability, propensity to compete for IgE binding with individual milk allergens, and ability to bind IgG4 from allergic and milk-tolerant individuals. The majority of milk SDRPs originated from caseins (97% of peptides) and overlapped with the known IgE epitopes of cow's milk allergens. SDRPs competed with milk proteins for binding to human IgE and readily formed aggregates. The average peptide length was 10.6 +/- 3.5 amino acids. The ability to provoke allergenic in vivo responses was confirmed by skin-prick testing (SPT) in five milk-allergic subjects. This was attributed to the peptide ability to aggregate into non-covalent complexes. SDRPs are able to induce response in SPT, but only in 50% of the sera SDRPs were able to inhibit IgG4 binding to caseins. Hence, SDRPs corresponding to the mainly continuous epitopes of milk proteins induce allergenic in vivo responses in milk-allergic subjects due to aggregation.",
publisher = "MDPI, Basel",
journal = "Foods",
title = "Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation",
number = "11",
volume = "9",
doi = "10.3390/foods9111576",
url = "conv_485"
}
Radosavljević, J., Apostolović, D., Mihailović, J., Atanasković-Marković, M., Burazer, L., van Hage, M.,& Ćirković-Veličković, T.. (2020). Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation. in Foods
MDPI, Basel., 9(11).
https://doi.org/10.3390/foods9111576
conv_485
Radosavljević J, Apostolović D, Mihailović J, Atanasković-Marković M, Burazer L, van Hage M, Ćirković-Veličković T. Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation. in Foods. 2020;9(11).
doi:10.3390/foods9111576
conv_485 .
Radosavljević, Jelena, Apostolović, Danijela, Mihailović, Jelena, Atanasković-Marković, Marina, Burazer, Lidija, van Hage, Marianne, Ćirković-Veličković, Tanja, "Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation" in Foods, 9, no. 11 (2020),
https://doi.org/10.3390/foods9111576 .,
conv_485 .
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