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Site-specific characterization of SARS-CoV-2 spike glycoprotein receptor-binding domain.

Authors
  • Antonopoulos, Aristotelis1
  • Broome, Steven2
  • Sharov, Victor2
  • Ziegenfuss, Christopher2
  • Easton, Richard L3
  • Panico, Maria1, 2, 3
  • Dell, Anne1
  • Morris, Howard R1, 2, 3
  • Haslam, Stuart M1
  • 1 Department of Life Sciences, Imperial College London, London, SW7 2AZ, UK.
  • 2 BioPharmaSpec Inc, 363 Phoenixville Pike, Malvern, PA 19355, USA.
  • 3 BioPharmaSpec Ltd, Suite 3.1, Lido Medical Centre, St. Saviour, Jersey, JE2 7LA, UK. , (Jersey)
Type
Published Article
Journal
Glycobiology
Publisher
Oxford University Press
Publication Date
Apr 01, 2021
Volume
31
Issue
3
Pages
181–187
Identifiers
DOI: 10.1093/glycob/cwaa085
PMID: 32886791
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

The novel coronavirus SARS-CoV-2, the infective agent causing COVID-19, is having a global impact both in terms of human disease as well as socially and economically. Its heavily glycosylated spike glycoprotein is fundamental for the infection process, via its receptor-binding domains interaction with the glycoprotein angiotensin-converting enzyme 2 on human cell surfaces. We therefore utilized an integrated glycomic and glycoproteomic analytical strategy to characterize both N- and O- glycan site-specific glycosylation within the receptor-binding domain. We demonstrate the presence of complex-type N-glycans with unusual fucosylated LacdiNAc at both sites N331 and N343 and a single site of O-glycosylation on T323. © The Author(s) 2020. Published by Oxford University Press.

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