Synthetic O-acetylated sialosides facilitate functional receptor identification for human respiratory viruses

Zeshi Li; Yifei Lang; Lin Liu; Mehman I Bunyatov; Angelic Isaza Sarmiento; Raoul J de Groot; Geert-Jan Boons

doi:10.1038/s41557-021-00655-9

Synthetic O-acetylated sialosides facilitate functional receptor identification for human respiratory viruses

Zeshi Li, Yifei Lang, Lin Liu, Mehman I Bunyatov, Angelic Isaza Sarmiento, Raoul J de Groot, Geert-Jan Boons

Utrecht University, University Medical Center Utrecht

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

The transmission of viruses from animal reservoirs to humans poses major threats to public health. Preparedness for future zoonotic outbreaks requires a fundamental understanding of how viruses of animal origin have adapted to binding to a cell surface component and/or receptor of the new host. Here we report on the specificities of human and animal viruses that engage with O-acetylated sialic acid, which include betacoronaviruses, toroviruses and influenza C and D viruses. Key to these studies was the development of a chemoenzymatic methodology that can provide almost any sialate-acetylation pattern. A collection of O-acetylated sialoglycans was printed as a microarray for the determination of receptor specificity. These studies showed host-specific patterns of receptor recognition and revealed that three distinct human respiratory viruses uniquely bind 9-O-acetylated α2,8-linked disialoside. Immunofluorescence and cell entry studies support that such a glycotope as part of a ganglioside is a functional receptor for human coronaviruses. [Figure not available: see fulltext.]

Original language	English
Pages (from-to)	496-503
Number of pages	8
Journal	Nature Chemistry
Volume	13
Issue number	5
Early online date	22 Mar 2021
DOIs	https://doi.org/10.1038/s41557-021-00655-9
Publication status	Published - May 2021

Bibliographical note

Funding Information:
We thank D. van Riel and L. M. E. Leijten (Erasmus MC) for providing the formalin-fixed paraffin-embedded human tissue sections, R. Wubbolts (Utrecht University) for offering guidance on confocal fluorescence microscopy and H. Egberink and S. Zhao (Utrecht University) for providing plasmids of the ECoV spike protein. This work was supported by TOP-PUNT Grant 718.015.003 of the Netherlands Organization for Scientific Research (G.-J.B.), ECHO Grant 711.011.006 of the Council for Chemical Sciences of the Netherlands Organization for Scientific Research (R.J.d.G.) and China Scholarship Council 2014-03250042 (Y.L.).

Publisher Copyright:
© 2021, The Author(s), under exclusive licence to Springer Nature Limited.

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10.1038/s41557-021-00655-9

s41557-021-00655-9Final published version, 3.37 MBLicence: Taverne

Cite this

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abstract = "The transmission of viruses from animal reservoirs to humans poses major threats to public health. Preparedness for future zoonotic outbreaks requires a fundamental understanding of how viruses of animal origin have adapted to binding to a cell surface component and/or receptor of the new host. Here we report on the specificities of human and animal viruses that engage with O-acetylated sialic acid, which include betacoronaviruses, toroviruses and influenza C and D viruses. Key to these studies was the development of a chemoenzymatic methodology that can provide almost any sialate-acetylation pattern. A collection of O-acetylated sialoglycans was printed as a microarray for the determination of receptor specificity. These studies showed host-specific patterns of receptor recognition and revealed that three distinct human respiratory viruses uniquely bind 9-O-acetylated α2,8-linked disialoside. Immunofluorescence and cell entry studies support that such a glycotope as part of a ganglioside is a functional receptor for human coronaviruses. [Figure not available: see fulltext.]",

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Synthetic O-acetylated sialosides facilitate functional receptor identification for human respiratory viruses

Abstract

Bibliographical note

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