Journal
JOURNAL OF VIROLOGY
Volume 79, Issue 1, Pages 632-636Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.79.1.632-636.2005
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Funding
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI046998] Funding Source: NIH RePORTER
- NIAID NIH HHS [R01 AI46998, R01 AI046998] Funding Source: Medline
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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.
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