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Hsp90 inhibitors reduce influenza virus replication in cell culture

Geoffrey Chase1, Tao Deng, Ervin Fodor

  • 1Department of Virology, Institute for Medical Microbiology and Hygiene, University of Freiburg, Hermann-Herder-Strasse 11, D-79104 Freiburg, Germany.

Virology
|June 24, 2008
PubMed

Insights

Heat shock protein 90 (Hsp90) inhibitors delay influenza A virus growth by disrupting viral polymerase complex assembly. This suggests Hsp90 inhibitors are a potential new class of antiviral drugs against influenza.

Area of Science:

  • Virology
  • Molecular Biology
  • Drug Discovery

Background:

  • Influenza A virus polymerase complex comprises PB1, PB2, and PA subunits.
  • Cellular chaperone Hsp90 aids polymerase complex nuclear import and assembly by binding PB1 and PB2.

Purpose of the Study:

  • To investigate the effect of Hsp90 inhibitors on influenza A virus replication.
  • To explore Hsp90 inhibitors as potential antiviral agents.

Main Methods:

  • Utilized Hsp90 inhibitors (geldanamycin, 17-AAG) in cell culture.
  • Assessed viral growth and viral titre.
  • Examined the impact on polymerase subunit stability and nuclear import.

Main Results:

  • Hsp90 inhibitors reduced influenza virus titre by 1-2 logs early in infection.
  • Inhibitors decreased the half-life of PB1 and PB2 subunits.
  • Nuclear import of PB1 and PA was inhibited, impairing viral RNP assembly.

Conclusions:

  • Hsp90 inhibition disrupts influenza virus replication by affecting polymerase complex formation.
  • Hsp90 inhibitors demonstrate potential as a novel antiviral strategy against influenza viruses.

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