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

• Published in: Glycobiology (Oxford) Vol. 31; no. 3; pp. 181 - 187
• Main Authors: Antonopoulos, Aristotelis, Broome, Steven, Sharov, Victor, Ziegenfuss, Christopher, Easton, Richard L, Panico, Maria, Dell, Anne, Morris, Howard R, Haslam, Stuart M
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01-04-2021
• Subjects: Angiotensin-Converting Enzyme 2 - chemistry; Angiotensin-Converting Enzyme 2 - metabolism; Binding Sites - genetics; Carbohydrate Conformation; Carbohydrate Sequence; Communication; COVID-19 - metabolism; COVID-19 - virology; Editor's Choice; Glycomics; Glycosylation; HEK293 Cells; Host Microbial Interactions; Humans; Pandemics; Protein Binding; Protein Interaction Domains and Motifs; Proteomics; Receptors, Virus - chemistry; Receptors, Virus - metabolism; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; SARS-CoV-2 - chemistry; SARS-CoV-2 - genetics; SARS-CoV-2 - metabolism; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spike Glycoprotein, Coronavirus - chemistry; Spike Glycoprotein, Coronavirus - genetics; Spike Glycoprotein, Coronavirus - metabolism; glycoproteomics; mass spectrometry; SARS-CoV-2; spike glycoprotein
• ISSN: 1460-2423; 0959-6658; 1460-2423
• DOI: 10.1093/glycob/cwaa085

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.