Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
3425498 | Virology | 2008 | 9 Pages |
Abstract
The viral RNA polymerase complex of influenza A virus consists of three subunits PB1, PB2 and PA. Recently, the cellular chaperone Hsp90 was shown to play a role in nuclear import and assembly of the trimeric polymerase complex by binding to PB1 and PB2. Here we show that Hsp90 inhibitors, geldanamycin or its derivative 17-AAG, delay the growth of influenza virus in cell culture resulting in a 1–2 log reduction in viral titre early in infection. We suggest that this is caused by the reduced half-life of PB1 and PB2 and inhibition of nuclear import of PB1 and PA which lead to reduction in viral RNP assembly. Hsp90 inhibitors may represent a new class of antiviral compounds against influenza viruses.
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Authors
Geoffrey Chase, Tao Deng, Ervin Fodor, Bo Wah Leung, Daniel Mayer, Martin Schwemmle, George Brownlee,