A facile chemoenzymatic synthesis of SARS-CoV-2 glycopeptides for probing glycosylation functions

Glycosylation plays important roles in SARS-CoV-2 infection. We describe here a facile chemoenzymatic synthesis of core-fucosylated N -glycopeptides derived from the SARS-CoV-2 Spike protein and their binding with glycan-dependent neutralizing antibody S309 and human lectin CLEC4G. The synthetic gly...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2021-07, Vol.57 (55), p.684-687
Main Authors: Zong, Guanghui, Li, Chao, Prabhu, Sunaina Kiran, Zhang, Roushu, Zhang, Xiao, Wang, Lai-Xi
Format: Article
Language:English
Subjects:
Antibiotics
Antibodies
Glycan
Glycopeptides
Glycosylation
Severe acute respiratory syndrome coronavirus 2
Synthesis
Viral diseases
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Summary:Glycosylation plays important roles in SARS-CoV-2 infection. We describe here a facile chemoenzymatic synthesis of core-fucosylated N -glycopeptides derived from the SARS-CoV-2 Spike protein and their binding with glycan-dependent neutralizing antibody S309 and human lectin CLEC4G. The synthetic glycopeptides provide tools for further functional characterization of viral glycosylation. Structurally well-defined synthetic SARS-CoV-2 glycopeptides provide useful probes for characterizing the glycan binding specificity of lectin and neutralizing antibody.
ISSN:1359-7345
1364-548X
DOI:10.1039/d1cc02790e