Glycosylation in SARS-CoV-2 Variants: A Path to Infection and Recovery

Overview

Journal Biochem Pharmacol

Specialties Biochemistry
Pharmacology

Date 2022 Nov 3

PMID 36328134

Authors

Arya Aloor

Rajaguru Aradhya

Parvathy Venugopal

Bipin Gopalakrishnan Nair

Renuka Suravajhala

Affiliations

Soon will be listed here.

Abstract

Glycan is an essential molecule that controls and drives life in a precise direction. The paucity of research in glycobiology may impede the significance of its role in the pandemic guidelines. The SARS-CoV-2 spike protein is heavily glycosylated, with 22 putative N-glycosylation sites and 17 potential O-glycosylation sites discovered thus far. It is the anchor point to the host cell ACE2 receptor, TMPRSS2, and many other host proteins that can be recognized by their immune system; hence, glycosylation is considered the primary target of vaccine development. Therefore, it is essential to know how this surface glycan plays a role in viral entry, infection, transmission, antigen, antibody responses, and disease progression. Although the vaccines are developed and applied against COVID-19, the proficiency of the immunizations is not accomplished with the current mutant variations. The role of glycosylation in SARS-CoV-2 and its receptor ACE2 with respect to other putative cell glycan receptors and the significance of glycan in host cell immunity in COVID-19 are discussed in this paper. Hence, the molecular signature of the glycan in the coronavirus infection can be incorporated into the mainstream therapeutic process.

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