Glycosylation of hepatitis C virus envelope proteins

Biochimie. Mar-Apr 2003;85(3-4):295-301. doi: 10.1016/s0300-9084(03)00004-x.

Abstract

Enveloped viruses are surrounded by a membrane derived from the host-cell that contains proteins called "envelope proteins". These proteins play a major role in virus assembly and entry. In most of the enveloped viruses, they are modified by N-linked glycosylation which is supposed to play a role in their stability, antigenicity and biological functions. Glycosylation is also known to play a major role in the biogenesis of proteins by being directly and/or indirectly involved in protein folding. Recent studies on hepatitis C virus (HCV) envelope proteins have revealed a complex interplay between cleavage by signal peptidase, folding and glycosylation. The knowledge that has been accumulated on the early steps of glycosylation of these proteins is presented in this review.

Publication types

  • Review

MeSH terms

  • Binding Sites
  • Glycoproteins / chemistry
  • Glycoproteins / metabolism
  • Glycosylation
  • Hepacivirus / metabolism*
  • Humans
  • In Vitro Techniques
  • Models, Biological
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism
  • Protein Processing, Post-Translational
  • Viral Envelope Proteins / chemistry
  • Viral Envelope Proteins / metabolism*

Substances

  • E1 protein, Hepatitis C virus
  • Glycoproteins
  • Polysaccharides
  • Viral Envelope Proteins
  • glycoprotein E2, Hepatitis C virus