1999/07/02 by Deborah R. Taylor, Stephanie T. Shi, Patrick R. Romano +2 · 2 citations
Biochemistry, Genetics and Molecular Biology · Medicine · #RNA regulation and disease #Viral Infections and Immunology Research #Endoplasmic Reticulum Stress and Disease
paper · doi:10.1126/science.285.5424.107
openalex publication_date 1999/07/02 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/23
Most isolates of hepatitis C virus (HCV) infections are resistant to interferon, the only available therapy, but the mechanism underlying this resistance has not been defined. Here it is shown that the HCV envelope protein E2 contains a sequence identical with phosphorylation sites of the interferon-inducible protein kinase PKR and the translation initiation factor eIF2alpha, a target of PKR. E2 inhibited the kinase activity of PKR and blocked its inhibitory effect on protein synthesis and cell growth. This interaction of E2 and PKR may be one mechanism by which HCV circumvents the antiviral effect of interferon.