AIP1/ALIX Is a Binding Partner for HIV-1 p6 and EIAV p9 Functioning in Virus Budding

• Published in: Cell Vol. 114; no. 6; pp. 689 - 699
• Main Authors: Strack, Bettina, Calistri, Arianna, Craig, Stewart, Popova, Elena, Göttlinger, Heinrich G
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 19.09.2003
• Subjects: Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - metabolism; Binding Sites - genetics; Cell Membrane - metabolism; Cell Membrane - virology; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Endosomal Sorting Complexes Required for Transport; gag Gene Products, Human Immunodeficiency Virus; Gene Products, gag - genetics; Gene Products, gag - metabolism; HeLa Cells; HIV-1 - genetics; HIV-1 - metabolism; Humans; Infectious Anemia Virus, Equine - genetics; Infectious Anemia Virus, Equine - metabolism; Microfilament Proteins - genetics; Microfilament Proteins - metabolism; Microscopy, Electron; Nuclear Proteins - genetics; Nuclear Proteins - metabolism; Protein Binding - genetics; Protein Structure, Tertiary - genetics; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Simian Immunodeficiency Virus - genetics; Simian Immunodeficiency Virus - metabolism; Transcription Factors - genetics; Transcription Factors - metabolism; Virus Shedding - physiology
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/S0092-8674(03)00653-6

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.