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Journal of Virology, September 2006, p. 9039-9052, Vol. 80, No. 18
0022-538X/06/$08.00+0     doi:10.1128/JVI.01013-06

Proteomic and Biochemical Analysis of Purified Human Immunodeficiency Virus Type 1 Produced from Infected Monocyte-Derived Macrophages

Elena Chertova,1* Oleg Chertov,2 Lori V. Coren,1 James D. Roser,1 Charles M. Trubey,1 Julian W. Bess Jr.,1 Raymond C. Sowder II,1 Eugene Barsov,1 Brian L. Hood,2 Robert J. Fisher,2 Kunio Nagashima,2 Thomas P. Conrads,2 Timothy D. Veenstra,2 Jeffrey D. Lifson,1 and David E. Ott1

AIDS Vaccine Program, Basic Research Program,1 Research Technology Program, SAIC—Frederick, Inc., NCI—Frederick, Frederick, Maryland 217022

Received 17 May 2006/ Accepted 24 June 2006

Human immunodeficiency virus type 1 (HIV-1) infects CD4+ T lymphocytes and monocytes/macrophages, incorporating host proteins in the process of assembly and budding. Analysis of the host cell proteins incorporated into virions can provide insights into viral biology. We characterized proteins in highly purified HIV-1 virions produced from human monocyte-derived macrophages (MDM), within which virus buds predominantly into intracytoplasmic vesicles, in contrast to the plasmalemmal budding of HIV-1 typically seen with infected T cells. Liquid chromatography-linked tandem mass spectrometry of highly purified virions identified many cellular proteins, including 33 previously described proteins in HIV-1 preparations from other cell types. Proteins involved in many different cellular structures and functions were present, including those from the cytoskeleton, adhesion, signaling, intracellular trafficking, chaperone, metabolic, ubiquitin/proteasomal, and immune response systems. We also identified annexins, annexin-binding proteins, Rab proteins, and other proteins involved in membrane organization, vesicular trafficking, and late endosomal function, as well as apolipoprotein E, which participates in cholesterol transport, immunoregulation, and modulation of cell growth and differentiation. Several tetraspanins, markers of the late endosomal compartment, were also identified. MDM-derived HIV contained 26 of 37 proteins previously found in exosomes, consistent with the idea that HIV uses the late endosome/multivesicular body pathway during virion budding from macrophages.

* Corresponding author. Mailing address: AIDS Vaccine Research Program, SAIC—Frederick, Inc., NCI—Frederick, Frederick, MD 21702. Phone: (301) 846-1455. Fax: (301) 846-5588. E-mail: chertova{at}ncifcrf.gov.

Journal of Virology, September 2006, p. 9039-9052, Vol. 80, No. 18
0022-538X/06/$08.00+0     doi:10.1128/JVI.01013-06




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