[Role of N-linked glycans in the functions of hepatitis C virus envelope glycoproteins].
Hepatitis C virus (HCV) is an enveloped virus and encodes two envelope glycoproteins, E1 and E2. E1 and E2 are transmembrane type I proteins with a N-terminal ectodomain and C-terminal anchor. During their synthesis, E1 and E2 ectodomains are targeted in the endoplasmic reticulum lumen where they are modified by N-linked glycosylation. After their synthesis, E1 and E2 assemble as a non-covalent heterodimer. The N-linked glycosylation is based on the recognition of specific asparagine residue in the context of the consensus sequence Asn-X-Ser/Thr. E1 contains potentially 4 or 5 N-linked glycosylation sites and E2 up to 11. Recent data indicated that some glycans of glycoproteins E1 and E2 play a major role in protein folding and heterodimer formation. Some N-linked glycans of E2 were involved in interactions with CD81, a putative cellular receptor for HCV. It appeared that N-linked glycans of E1 and E2 played an important role of in the viral entry.
Goffard
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A
Service de virologie, UPRES-EA3610, CHRU Lille, Faculté de médecine, Université Lille 2, Lille, France. a-goffard@chru-lille.fr
Lazrek
M
M
Bocket
L
L
Dewilde
A
A
Hober
D
D
D006031:Glycosylation; D016174:Hepacivirus / Q000378:metabolism* / Q000472:pathogenicity; D011134:Polysaccharides / Q000502:physiology*; D014759:Viral Envelope Proteins / Q000502:physiology*
D011134:Polysaccharides; D014759:Viral Envelope Proteins