Kanazir, Danijela

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  • Kanazir, Danijela (1)
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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
UR  - conv_468
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",
url = "conv_468"
}
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
conv_468
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
conv_468 .
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 .,
conv_468 .
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