Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein
DR Taylor, ST Shi, PR Romano, GN Barber, MMC Lai - Science, 1999 - science.org
DR Taylor, ST Shi, PR Romano, GN Barber, MMC Lai
Science, 1999•science.orgMost 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 eIF2α, 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 …
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 eIF2α, 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 …
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 eIF2α, 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.
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