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A facile chemoenzymatic synthesis of SARS-CoV-2 glycopeptides for probing glycosylation functions.
Zong, Guanghui; Li, Chao; Prabhu, Sunaina Kiran; Zhang, Roushu; Zhang, Xiao; Wang, Lai-Xi.
  • Zong G; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA. wang518@umd.edu.
  • Li C; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA. wang518@umd.edu.
  • Prabhu SK; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA. wang518@umd.edu.
  • Zhang R; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA. wang518@umd.edu.
  • Zhang X; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA. wang518@umd.edu.
  • Wang LX; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA. wang518@umd.edu.
Chem Commun (Camb) ; 57(55): 6804-6807, 2021 Jul 08.
Article in English | MEDLINE | ID: covidwho-1284708
ABSTRACT
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Glycopeptides / Spike Glycoprotein, Coronavirus Language: English Journal: Chem Commun (Camb) Journal subject: Chemistry Year: 2021 Document Type: Article Affiliation country: D1cc02790e

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Glycopeptides / Spike Glycoprotein, Coronavirus Language: English Journal: Chem Commun (Camb) Journal subject: Chemistry Year: 2021 Document Type: Article Affiliation country: D1cc02790e