Details

Autor(en) / Beteiligte

• Goffard, A
• Lazrek, M
• Bocket, L
• Dewilde, A
• Hober, D

Titel

Role of N-linked glycans in the functions of hepatitis C virus envelope glycoproteins

Ist Teil von

• Annales de biologie clinique (Paris), 2007-05, Vol.65 (3), p.237-246

Ort / Verlag

France: John Libbey Eurotext

Erscheinungsjahr

2007

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.