Recombinant SARS-CoV-2 S Protein Binds to Glycans of the Lactosamine Family in vitro

Many viruses, beside binding to their main cell target, interact with other molecules that promote virus adhesion to the cell; often, these additional targets are glycans. The main receptor for SARS-CoV-2 is a peptide motif in the ACE2 protein. We studied interaction of the recombinant SARS-CoV-2 sp...

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Detalles Bibliográficos
Autores principales: Ryzhikov, Alexandr B., Onkhonova, Galina S., Imatdinov, Ilnaz R., Gavrilova, Elena V., Maksyutov, Rinat A., Gordeeva, Elena A., Pazynina, Galina V., Ryzhov, Ivan M., Shilova, Nadezhda V., Bovin, Nicolai V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Pleiades Publishing 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7905424/
https://www.ncbi.nlm.nih.gov/pubmed/33838626
http://dx.doi.org/10.1134/S0006297921030019
Descripción
Sumario:Many viruses, beside binding to their main cell target, interact with other molecules that promote virus adhesion to the cell; often, these additional targets are glycans. The main receptor for SARS-CoV-2 is a peptide motif in the ACE2 protein. We studied interaction of the recombinant SARS-CoV-2 spike (S) protein with an array of glycoconjugates, including various sialylated, sulfated, and other glycans, and found that the S protein binds some (but not all) glycans of the lactosamine family. We suggest that parallel influenza infection will promote SARS-CoV-2 adhesion to the respiratory epithelial cells due to the unmasking of lactosamine chains by the influenza virus neuraminidase. ELECTRONIC SUPPLEMENTARY MATERIAL: Supplementary material is available in the online version of this article at 10.1134/S0006297921030019 and on the journal website (http://protein.bio.msu.ru/biokhimiya).

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