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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.

Original publication

DOI

10.1016/j.virol.2008.04.040

Type

Journal article

Journal

Virology

Publication Date

01/08/2008

Volume

377

Pages

431 - 439

Keywords

Benzoquinones, Cell Culture Techniques, HSP90 Heat-Shock Proteins, Humans, Influenza A virus, Lactams, Macrocyclic, RNA Replicase, Viral Proteins, Virus Assembly, Virus Replication