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Blood, 15 September 2004, Vol. 104, No. 6, pp. 1867-1872. Prepublished online as a Blood First Edition Paper on May 27, 2004; DOI 10.1182/blood-2004-01-0081. This Article Full Text Full Text (PDF) All Versions of this Article: 2004-01-0081v1 104/6/1867    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Iordanskiy, S. Articles by Bukrinsky, M. Search for Related Content PubMed PubMed Citation Articles by Iordanskiy, S. Articles by Bukrinsky, M. Related Collections Phagocytes Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  PHAGOCYTES Heat-shock protein 70 exerts opposing effects on Vpr-dependent and Vpr-independent HIV-1 replication in macrophages Sergey Iordanskiy, Yuqi Zhao, Paola DiMarzio, Isabelle Agostini, Larisa Dubrovsky, and Michael Bukrinsky From the George Washington University, Washington, DC; Northwestern University Feinberg School of Medicine, Chicago, IL; the North Shore–Long Island Jewish Research Institute, Manhasset, NY; and D. I. Ivanovsky Institute of Virology, Moscow, Russia. HIV-1 viral protein R (Vpr) shuttles between the nucleus and the cytoplasm and is believed to contribute to the process of nuclear translocation of the viral preintegration complex, thus facilitating HIV-1 replication in macrophages. In this report, we demonstrate that Hsp70, a heat-shock protein contributing to cellular stress responses, inhibits nuclear translocation of HIV-1 Vpr. In macrophages, Hsp70 is induced shortly after HIV-1 infection. Recombinant Hsp70 or a mild heat shock diminished replication of the wild-type HIV-1, suggesting that Hsp70 might function as an innate antiviral factor. Surprisingly, Hsp70 stimulated nuclear import and replication in macrophages of the Vpr-deficient HIV-1 construct. This finding suggests that Hsp70 and Vpr may function in a similar manner when expressed separately, but they neutralize each other's activity when present together. Consistent with this interpretation, Hsp70 coprecipitated with Vpr from HIV-1–infected cells. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: E. Acheampong, Z. Parveen, A. Mengistu, N. Ngoubilly, B. Wigdahl, A. S. Lossinsky, R. J. Pomerantz, and M. Mukhtar Cholesterol-Depleting Statin Drugs Protect Postmitotically Differentiated Human Neurons against Ethanol- and Human Immunodeficiency Virus Type 1-Induced Oxidative Stress In Vitro J. Virol., February 1, 2007; 81(3): 1492 - 1501. [Abstract] [Full Text] [PDF] A. Varin, A.-Z. Decrion, E. Sabbah, V. Quivy, J. Sire, C. Van Lint, B. P. Roques, B. B. Aggarwal, and G. Herbein Synthetic Vpr Protein Activates Activator Protein-1, c-Jun N-terminal Kinase, and NF-{kappa}B and Stimulates HIV-1 Transcription in Promonocytic Cells and Primary Macrophages J. Biol. Chem., December 30, 2005; 280(52): 42557 - 42567. [Abstract] [Full Text] [PDF]

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