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Journal of Virology, January 2005, p. 632-636, Vol. 79, No. 1
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.1.632-636.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Human Immunodeficiency Virus Type 1 Nef Domains Required for Disruption of Major Histocompatibility Complex Class I Trafficking Are Also Necessary for Coprecipitation of Nef with HLA-A2

Maya Williams,1 Jeremiah F. Roeth,1 Matthew R. Kasper,2 Tracey M. Filzen,3 and Kathleen L. Collins1,2,3*

Graduate Program in Cellular and Molecular Biology,1 Department of Microbiology and Immunology,2 Department of Internal Medicine, The University of Michigan, Ann Arbor, Michigan3

Received 11 June 2004/ Accepted 26 August 2004

Human immunodeficiency virus type 1 (HIV-1) Nef is a critical protein that is necessary for HIV pathogenesis. Its roles include the disruption of major histocompatibility complex class I (MHC-I) and CD4 trafficking to promote immune evasion and viral spread. Mutational analyses have revealed that separate domains of Nef are required to affect these two molecules. To further elucidate how Nef disrupts MHC-I trafficking in T cells, we examined the role of protein domains that are required for this function (N-terminal alpha helix, polyproline, acidic, and oligomerization domains). We found that each of these regions was required for Nef to disrupt the transport of HLA-A2 to the cell surface and for Nef to coprecipitate with HLA-A2.


* Corresponding author. Mailing address: Department of Internal Medicine, The University of Michigan, 4301 MSRBIII, Box 0638, 1150 West Medical Center Dr., Ann Arbor, MI 48109. Phone: (734) 615-1320. Fax: (734) 763-7672. E-mail: klcollin{at}umich.edu.


Journal of Virology, January 2005, p. 632-636, Vol. 79, No. 1
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.1.632-636.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




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