Open Access
International Journal of Molecular Sciences, volume 23, issue 1, pages 557
Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers
Grabovenko Fedor
1
,
Абросимова Л. А.
1
,
Yanenko Bogdan
2
,
Ulitin Andrey
2
,
Zatsepin Timofei S.
1, 3
,
Zavyalova Elena
1
,
2
Biogenec Joint-Stock Company, Moscow Region, 142290 Pushchino, Russia
|
Publication type: Journal Article
Publication date: 2022-01-05
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 5.6
ISSN: 16616596, 14220067
PubMed ID:
35008982
Catalysis
Organic Chemistry
Inorganic Chemistry
Physical and Theoretical Chemistry
Computer Science Applications
Spectroscopy
Molecular Biology
General Medicine
Abstract
Nucleic acid aptamers specific to S-protein and its receptor binding domain (RBD) of SARS-CoV-2 (severe acute respiratory syndrome-related coronavirus 2) virions are of high interest as potential inhibitors of viral infection and recognizing elements in biosensors. Development of specific therapy and biosensors is complicated by an emergence of new viral strains bearing amino acid substitutions and probable differences in glycosylation sites. Here, we studied affinity of a set of aptamers to two Wuhan-type RBD of S-protein expressed in Chinese hamster ovary cell line and Pichia pastoris that differ in glycosylation patterns. The expression system for the RBD protein has significant effects, both on values of dissociation constants and relative efficacy of the aptamer binding. We propose glycosylation of the RBD as the main force for observed differences. Moreover, affinity of a several aptamers was affected by a site of biotinylation. Thus, the robustness of modified aptamers toward new virus variants should be carefully tested.
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Citations by publishers
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2 publications, 22.22%
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2 publications, 22.22%
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1 publication, 11.11%
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1 publication, 11.11%
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Springer Nature
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Springer Nature
1 publication, 11.11%
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1
2
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Grabovenko F. et al. Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers // International Journal of Molecular Sciences. 2022. Vol. 23. No. 1. p. 557.
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Grabovenko F., Абросимова Л. А., Yanenko B., Ulitin A., Loktyushov E., Zatsepin T. S., Zavyalova E., Zvereva M. Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers // International Journal of Molecular Sciences. 2022. Vol. 23. No. 1. p. 557.
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RIS
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TY - JOUR
DO - 10.3390/ijms23010557
UR - https://doi.org/10.3390%2Fijms23010557
TI - Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers
T2 - International Journal of Molecular Sciences
AU - Yanenko, Bogdan
AU - Ulitin, Andrey
AU - Grabovenko, Fedor
AU - Абросимова, Л. А.
AU - Loktyushov, Eugene
AU - Zatsepin, Timofei S.
AU - Zavyalova, Elena
AU - Zvereva, Maria
PY - 2022
DA - 2022/01/05 00:00:00
PB - Multidisciplinary Digital Publishing Institute (MDPI)
SP - 557
IS - 1
VL - 23
PMID - 35008982
SN - 1661-6596
SN - 1422-0067
ER -
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@article{2022_Grabovenko,
author = {Bogdan Yanenko and Andrey Ulitin and Fedor Grabovenko and Л. А. Абросимова and Eugene Loktyushov and Timofei S. Zatsepin and Elena Zavyalova and Maria Zvereva},
title = {Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers},
journal = {International Journal of Molecular Sciences},
year = {2022},
volume = {23},
publisher = {Multidisciplinary Digital Publishing Institute (MDPI)},
month = {jan},
url = {https://doi.org/10.3390%2Fijms23010557},
number = {1},
pages = {557},
doi = {10.3390/ijms23010557}
}
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MLA
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Grabovenko, Fedor, et al. “Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers.” International Journal of Molecular Sciences, vol. 23, no. 1, Jan. 2022, p. 557. https://doi.org/10.3390%2Fijms23010557.
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