ELLSA based profiling of surface glycosylation in microorganisms reveals that ß-glucan rich yeasts’ surfaces are selectively recognized with recombinant banana lectin
Authorized Users Only
2020
Authors
Dragačević, LukaĐorđević, Brižita

Gavrović-Jankulović, Marija
Ilić, Vesna

Kanazir, Danijela
Minić, Rajna

Article (Published version)

Metadata
Show full item recordAbstract
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, RCA120 - 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 RCA120 wh...ich 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 μg mL−1 and to P. roqueforti with 1.10 μg mL−1. This unique specificity of BL could be exploited for screening purposes and potentially for the detection of ß-glucan in solutions.
Keywords:
Banana lectin / ELLSA / Fungi / Glycosylation / MicroorganismsSource:
Glycoconjugate Journal, 2020, 37, 1, 95-105Publisher:
- Springer Nature
Funding / projects:
- Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance (RS-172049)
- Palinspastika tektonostratigrafskih jedinica između Jadranske i Mezijske ploče (RS-146009)
DOI: 10.1007/s10719-019-09898-8
ISSN: 0282-0080
WoS: 000511535000008
Scopus: 2-s2.0-85076543208
Collections
Institution/Community
PharmacyTY - JOUR AU - Dragačević, Luka AU - Đorđević, Brižita AU - Gavrović-Jankulović, Marija AU - Ilić, Vesna AU - Kanazir, Danijela AU - Minić, Rajna PY - 2020 UR - https://farfar.pharmacy.bg.ac.rs/handle/123456789/3531 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, RCA120 - 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 RCA120 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 μg mL−1 and to P. roqueforti with 1.10 μg 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 Nature 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 VL - 37 IS - 1 SP - 95 EP - 105 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, RCA120 - 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 RCA120 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 μg mL−1 and to P. roqueforti with 1.10 μg 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 Nature", 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", volume = "37", number = "1", pages = "95-105", 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 Nature., 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 . .