Abstract
During their passage through endoplasmic reticulum and Golgi complex, proteins are subjected to modifications such as N-glycosylation. N-glycans play a pivotal role in protein folding and quality control of glycoproteins. Most of viral envelope proteins are N-glycosylated and use the cellular glycosylation machinery. The presence of glycans on envelope proteins gives several advantages to viruses. First it enables a correct folding of viral proteins. Moreover, glycans associated to envelope proteins can play a role the in viral entry process and help viruses to evade from the host immune system. Hepatits C Virus (HCV) E1 and E2 envelope proteins are highly N-glycosylated. Studies using retroviral particles pseudotyped with HCV envelope proteins and native virus produced in cell culture have shown that these glycans play an essential role in HCV life cycle. Furthermore, since these glycans are highly conserved and play a pivotal role, they constitute an interesting target for the development of new therapeutic strategies. This review summarizes the knowledge on the role of HCVenvelope.
Published Version
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