This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Parissi, V.
Right arrow Articles by Litvak, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Parissi, V.
Right arrow Articles by Litvak, S.

 Previous Article  |  Next Article 

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.


This article has been cited by other articles:

  • Lesbats, P., Metifiot, M., Calmels, C., Baranova, S., Nevinsky, G., Andreola, M. L., Parissi, V. (2008). In vitro initial attachment of HIV-1 integrase to viral ends: control of the DNA specific interaction by the oligomerization state. Nucleic Acids Res 36: 7043-7058 [Abstract] [Full Text]  
  • Mousnier, A., Kubat, N., Massias-Simon, A., Segeral, E., Rain, J.-C., Benarous, R., Emiliani, S., Dargemont, C. (2007). von Hippel Lindau binding protein 1-mediated degradation of integrase affects HIV-1 gene expression at a postintegration step. Proc. Natl. Acad. Sci. USA 104: 13615-13620 [Abstract] [Full Text]  
  • Desfarges, S., San Filippo, J., Fournier, M., Calmels, C., Caumont-Sarcos, A., Litvak, S., Sung, P., Parissi, V. (2006). Chromosomal integration of LTR-flanked DNA in yeast expressing HIV-1 integrase: down regulation by RAD51. Nucleic Acids Res 34: 6215-6224 [Abstract] [Full Text]  
  • Maroun, M., Delelis, O., Coadou, G., Bader, T., Segeral, E., Mbemba, G., Petit, C., Sonigo, P., Rain, J.-C., Mouscadet, J.-F., Benarous, R., Emiliani, S. (2006). Inhibition of Early Steps of HIV-1 Replication by SNF5/Ini1. J. Biol. Chem. 281: 22736-22743 [Abstract] [Full Text]  
  • Montano, M., Rarick, M., Sebastiani, P., Brinkmann, P., Skefos, J., Ericksen, R. (2006). HIV-1 burden influences host response to co-infection with Neisseria gonorrhoeae in vitro. Int Immunol 18: 125-137 [Abstract] [Full Text]  
  • Faure, A.él., Calmels, C., Desjobert, Céc., Castroviejo, M., Caumont-Sarcos, A., Tarrago-Litvak, L., Litvak, S., Parissi, V. (2005). HIV-1 integrase crosslinked oligomers are active in vitro. Nucleic Acids Res 33: 977-986 [Abstract] [Full Text]  
  • Cherepanov, P., Devroe, E., Silver, P. A., Engelman, A. (2004). Identification of an Evolutionarily Conserved Domain in Human Lens Epithelium-derived Growth Factor/Transcriptional Co-activator p75 (LEDGF/p75) That Binds HIV-1 Integrase. J. Biol. Chem. 279: 48883-48892 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»