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Journal of Virology, December 2001, p. 11344-11353, Vol. 75, No. 23
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.23.11344-11353.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Functional Interactions of Human Immunodeficiency Virus Type 1 Integrase with Human and Yeast HSP60

Vincent Parissi,1,2,* Christina Calmels,1,2 Vaea Richard De Soultrait,1,2 Anne Caumont,2,3 Michel Fournier,1,2 Stéphane Chaignepain,4 and Simon Litvak1,2

REGER, UMR-5097 Centre National de la Recherche Scientifique (CNRS)-Université Victor Segalen Bordeaux 2,1 Laboratoire de Virologie, Hôpital Pellegrin,3 IBGC-CNRS,4 and IFR66 Pathologies infectieuses,2 Bordeaux, France

Received 19 January 2001/Accepted 17 August 2001

Integration of human immunodeficiency virus type 1 (HIV-1) proviral DNA in the nuclear genome is catalyzed by the retroviral integrase (IN). In addition to IN, viral and cellular proteins associated in the high-molecular-weight preintegration complex have been suggested to be involved in this process. In an attempt to define host factors interacting with IN, we used an in vitro system to identify cellular proteins in interaction with HIV-1 IN. The yeast Saccharomyces cerevisiae was chosen since (i) its complete sequence has been established and the primary structure of all the putative proteins from this eucaryote has been deduced, (ii) there is a significant degree of homology between human and yeast proteins, and (iii) we have previously shown that the expression of HIV-1 IN in yeast induces a lethal phenotype. Strong evidences suggest that this lethality is linked to IN activity in infected human cells where integration requires the cleavage of genomic DNA. Using IN-affinity chromatography we identified four yeast proteins interacting with HIV-1 IN, including the yeast chaperonin yHSP60, which is the counterpart of human hHSP60. Yeast lethality induced by HIV-1 IN was abolished when a mutated HSP60 was coexpressed, therefore suggesting that both proteins interact in vivo. Besides interacting with HIV-1 IN, the hHSP60 was able to stimulate the in vitro processing and joining activities of IN and protected this enzyme from thermal denaturation. In addition, the functional human HSP60-HSP10 complex in the presence of ATP was able to recognize the HIV-1 IN as a substrate.

* Corresponding author. Mailing address: REGER, UMR-5097 CNRS-Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux Cedex, France. Phone: 33-(0)5 57 57 17 40. Fax: 33-(0)5 57 57 17 66. E-mail: vincent.parissi{at}reger.u-bordeaux2.fr.

Journal of Virology, December 2001, p. 11344-11353, Vol. 75, No. 23
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.23.11344-11353.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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