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Hsp90: a chaperone for HIV-1

Published online by Cambridge University Press:  24 April 2014

JUN SIONG LOW  and
ARIBERTO FASSATI
JUN SIONG LOW
Affiliation:
The Wohl Virion Centre, MRC Centre for Medical Molecular Virology, Division of Infection & Immunity, UCL, Cruciform Building, 90 Gower Street, London WC1E 6BT, UK
ARIBERTO FASSATI*
Affiliation:
The Wohl Virion Centre, MRC Centre for Medical Molecular Virology, Division of Infection & Immunity, UCL, Cruciform Building, 90 Gower Street, London WC1E 6BT, UK
*
*Corresponding author: The Wohl Virion Centre, MRC Centre for Medical Molecular Virology, Division of Infection & Immunity, UCL, Cruciform Building, 90 Gower Street, London WC1E 6BT, UK. E-mail: a.fassati@ucl.ac.uk
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Summary

HIV-1 replication has been intensively investigated over the past 30 years. Hsp90 is one of the most abundant proteins in human cells, important in the formation and function of several protein complexes that maintain cell homeostasis. Remarkably, the impact of Hsp90 on HIV-1 infection has started to be appreciated only recently. Hsp90 has been shown to (a) promote HIV-1 gene expression in acutely infected cells, (b) localize at the viral promoter DNA, (c) mediate enhanced replication in conditions of hyperthermia and (d) activate the P-TEFb complex, which is essential for efficient HIV-1 transcription. Hsp90 has been implicated in buffering deleterious mutations of the viral core and in the regulation of innate and acquired immune responses to HIV-1 infection. Therefore, Hsp90 is an important host factor promoting several steps of the HIV-1 life cycle. Several small Hsp90 inhibitors are in Phase II clinical trials for human cancers and might potentially be used to inhibit HIV-1 infection at multiple levels.

Keywords

HIV-1Hsp90transcriptionCdc37immunitydrugs
Type
Special Issue Article
Information
Parasitology , Volume 141 , Special Issue 9: Heat shock proteins as drug targets in infectious diseases , August 2014 , pp. 1192 - 1202
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Copyright
Copyright © Cambridge University Press 2014 

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