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Journal of Virology, May 2002, p. 4666-4670, Vol. 76, No. 9
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.9.4666-4670.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Specific Incorporation of Heat Shock Protein 70 Family Members into Primate Lentiviral Virions

Cagan Gurer,1 Andrea Cimarelli,2 and Jeremy Luban1*

Departments of Microbiology and Medicine, Columbia University College of Physicians and Surgeons, New York, New York 10032,1 Ecole Normale Supérieure de Lyon, 69364 Lyon, France2

Received 4 October 2001/ Accepted 28 January 2002

To determine if any heat shock proteins are incorporated into human immunodeficiency virus type 1 (HIV-1) virions in a manner similar to that of the peptidyl-prolyl isomerase cyclophilin A, we probed purified virions with antibodies against heat shock proteins Hsp27, Hsp40, Hsp60, Hsp70, Hsc70, and Hsp90. Of these proteins, Hsp60, Hsp70, and Hsc70 associated with virions purified based on either particle density or size and were shown to be incorporated within the virion membrane, where they were protected from digestion by exogenous protease. Virion incorporation of Hsp70 was also observed with HIV-2 and with simian immunodeficiency viruses SIVMAC and SIVAGM, but it appears to be specific for primate lentiviruses, since Hsp70 was not detected in association with Moloney murine leukemia virus virions. Of the HIV-1 genes, gag was found to be sufficient for Hsp70 incorporation, though Hsp70 was roughly equimolar with pol-encoded proteins in virions.

* Corresponding author. Mailing address: Departments of Microbiology and Medicine, Columbia University College of Physicians and Surgeons, 701 W. 168th St., New York, NY 10032. Phone: (212) 305-8706. Fax: (212) 305-0333. E-mail: JL45{at}columbia.edu.

Journal of Virology, May 2002, p. 4666-4670, Vol. 76, No. 9
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.9.4666-4670.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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