Glycosylation in SARS-CoV-2 variants: A path to infection and recovery

Biochem Pharmacol. 2022 Dec:206:115335. doi: 10.1016/j.bcp.2022.115335. Epub 2022 Oct 31.

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.

Keywords: Glycobiology; Glycosylation; Immunity; Vaccine development.

Publication types

  • Review

MeSH terms

  • Angiotensin-Converting Enzyme 2 / genetics
  • COVID-19*
  • Glycosylation
  • Humans
  • Polysaccharides / metabolism
  • SARS-CoV-2* / genetics

Substances

  • spike protein, SARS-CoV-2
  • Angiotensin-Converting Enzyme 2
  • Polysaccharides

Supplementary concepts

  • SARS-CoV-2 variants