AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding.

HIV-1 and other retroviruses exit infected cells by budding from the plasma membrane, a process requiring membrane fission. The primary late assembly (L) domain in the p6 region of HIV-1 Gag mediates the detachment of the virion by recruiting host Tsg101, a component of the class E vacuolar protein sorting ...
(Vps) machinery. We now show that HIV Gag p6 contains a second region involved in L domain function that binds AIP1, a homolog of the yeast class E Vps protein Bro1. Further, AIP1 interacts with Tsg101 and homologs of a subunit of the yeast class E Vps protein complex ESCRT-III. AIP1 also binds to the L domain in EIAV p9, and this binding correlates perfectly with L domain function. These observations identify AIP1 as a component of the viral budding machinery, which serves to link a distinct region in the L domain of HIV-1 p6 and EIAV p9 to ESCRT-III.
Mesh Terms:
Adenosine Triphosphatases, Binding Sites, Cell Membrane, DNA-Binding Proteins, Endosomal Sorting Complexes Required for Transport, Gene Products, gag, HIV-1, Hela Cells, Humans, Infectious Anemia Virus, Equine, Microfilament Proteins, Microscopy, Electron, Nuclear Proteins, Protein Binding, Protein Structure, Tertiary, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins, Simian immunodeficiency virus, Transcription Factors, Virus Shedding, gag Gene Products, Human Immunodeficiency Virus
Cell
Date: Sep. 19, 2003
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