Site-specific characterization of SARS-CoV-2 spike glycoprotein receptor-binding domain.
Glycobiology
; 31(3): 181-187, 2021 04 01.
Article
in English
| MEDLINE | ID: covidwho-1169666
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.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Spike Glycoprotein, Coronavirus
/
SARS-CoV-2
/
COVID-19
Limits:
Humans
Language:
English
Journal:
Glycobiology
Journal subject:
Biochemistry
Year:
2021
Document Type:
Article
Affiliation country:
Glycob
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