Glycosylation of the hepatitis C virus envelope protein E1 is dependent on the presence of a downstream sequence on the viral polyprotein.

The addition of N-linked oligosaccharides to Asn-X-(Ser/Thr) sites is catalyzed by the oligosaccharyltransferase, an enzyme closely associated with the translocon and generally thought to have access only to nascent chains as they emerge from the ribosome. However, the presence of the sequon does not automatically ensure core glycosylation because many proteins contain sequons that remain either nonglycosylated or glycosylated to a variable extent. In this study, hepatitis C virus (HCV) envelope protein E1 was used as a model to study the efficiency of N-glycosylation. HCV envelope proteins, E1 and E2, were released from a polyprotein precursor after cleavage by host signal peptidase(s). When expressed alone, E1 was not efficiently glycosylated. However, E1 glycosylation was improved when expressed as a polyprotein including full-length or truncated forms of E2. These data indicate that glycosylation of E1 is dependent on the presence of polypeptide sequences located downstream of E1 on HCV polyprotein.