Targeting conserved N-glycosylation blocks SARS-CoV-2 variant infection in vitro.

ABSTRACT:

Background

Despite clinical success with anti-spike vaccines, the effectiveness of neutralizing antibodies and vaccines has been compromised by rapidly spreading SARS-CoV-2 variants. Viruses can hijack the glycosylation machinery of host cells to shield themselves from the host's immune response and attenuate antibody efficiency. However, it remains unclear if targeting glycosylation on viral spike protein can impair infectivity of SARS-CoV-2 and its variants.

Methods

We adopted flow cytometry, ELISA, and BioLayer interferometry approaches to assess binding of glycosylated or deglycosylated spike with ACE2. Viral entry was determined by luciferase, immunoblotting, and immunofluorescence assays. Genome-wide association study (GWAS) revealed a significant relationship between

SUBMITTER: Huang HC 

PROVIDER: S-EPMC8613501 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature