Alterations in N-glycosylation of HCV E2 Protein in Children Patients with IFN-RBV Therapy Failure.

ABSTRACT: The glycosylation of viral envelope proteins plays an important role in virus biology and the immune response of the host to infection. Hepatitis C virus (HCV) envelope proteins E1 and E2, key players in virus entry and spread, are highly N-glycosylated and possess 4 (5 in certain genotypes) to 11 conserved glycosylation sites, respectively. Many published results based on recombinant proteins indicate that the glycan shield can mask the epitopes targeted by neutralizing antibodies. Glycan shifting within the conserved linear E2 region (412-423) could be one of the escape strategies used by HCV. In the present report, we isolated E2 genes from samples (collected before the IFN-RBV therapy) originating from pediatric patients infected with HCV gt 1a. We analyzed the biochemical properties o

SUBMITTER: Zimmer K 

PROVIDER: S-EPMC10974529 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature