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Envelope surface glycoprotein gp160, precursor
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env
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In the absence of Vpu, Env accumulates extensively within clathrin-coated endosomal structures, including the viral proteins Gag and MA; the tetraspanins CD63 and CD81; the adaptor protein complex AP-3; and AIP1/ALIX, a cellular cofactor for viral budding |
PubMed
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Nef
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nef
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HIV-1 Nef-mediated CD4 degradation requires ALIX and interaction of Nef with ALIX in endosomes that contain CD4 |
PubMed
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nef
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HIV-1 Nef interacts with ALIX in late endosomes, and Bro1 (residues 1-360) and V (residues 360-717) domains of ALIX are required for this interaction with Nef |
PubMed
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nef
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Residues 135-138 of HIV-1 Nef bind to AIP1 in vitro and in cells; the binding between Nef and AIP1 is required for formation of multivesicular bodies (MVBs) and contributes to the egress of viral particles from infected cells |
PubMed
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nef
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HIV-1 Nef increases the production of exosomes and co-localizes with exosomal proteins CD63, AIP/Alix, AChE, Hsc70, LAMP2, and annexin A2 in HeLa cells |
PubMed
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Pr55(Gag)
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gag
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HIV-1 NC-mediated incorporation of ALIX into virions requires the zinc fingers of NC and the Bro1 domain of ALIX |
PubMed
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gag
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Superresolution imaging of HIV-1 Gag and ESCRT proteins (TSG101, ALIX, CHMP4B, and CHMP4C) demonstrates in HeLa cells that Gag assemblages often has ESCRT proteins in their direct vicinity |
PubMed
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gag
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Galectin-3 co-localizes with HIV-1 Gag and Alix, and facilitates the association of Gag with Alix in cells |
PubMed
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gag
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Incorporation of ALIX into HIV-1 virus-like particles is dependent on the Gag late domains |
PubMed
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gag
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ALIX recruitment to both HIV-1 and EIAV Gag is transient at the end of Gag polymerization and the HIV-1 and EIAV profiles are only different in terms of the retention level of ALIX within the virus-like particles |
PubMed
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gag
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The Bro1 domain of Alix inhibits HIV budding by targeting both PTAP/TSG101 and LYPXnL/Alix pathways. The NC domain of Gag is the primary target for Bro1 inhibition by Gag-mediated recruitment of Bro1 to the plasma membrane |
PubMed
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gag
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The S40F mutation in HIV-1 p6 enhances ALIX binding to HIV-1 Gag in the yeast two-hybrid assay. The Y36S mutation introduced into the S40F mutant disrupts ALIX interaction with Gag and restores spherical particle formation in cells |
PubMed
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gag
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Fusion protein Dub-Alix, the catalytic domain of the Herpes Simplex UL36 deubiquitinating enzyme (DUb) fused onto Alix, inhibits HIV-1 release, which involves the interaction between HIV-1 Gag and Alix |
PubMed
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gag
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In the absence of Vpu, Env accumulates extensively within clathrin-coated endosomal structures, including the viral proteins Gag and MA; the tetraspanins CD63 and CD81; the adaptor protein complex AP-3; and AIP1/ALIX, a cellular cofactor for viral budding |
PubMed
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gag
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Alix-mediated rescue of HIV-1 PTAP(-) release requires interaction with Nedd4-1. Ubiquitinated Alix is incorporated into HIV-1 PTAP(-) rescued particles |
PubMed
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gag
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Phe105 loop (residues 99-112) in the Bro1 domain of Alix is required for efficient Alix-mediated HIV-1 release. The disruption of the Phe105 loop interferes with its ability to interact with HIV-1 Gag |
PubMed
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gag
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Recruitment of CHMP4B by ALIX to HIV-1 Gag puncta is observed in in-vitro membrane model |
PubMed
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gag
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ALIX proteins with point mutations (Val498Asp, Phe676Asp, and Ile683Asp) that inhibit the p6 36YPLASL41 binding fail to rescue HIV-1 deltaPTAP release or infectivity |
PubMed
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gag
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Overexpression of AIP1(364-716) severely disrupts Gag processing, resulting in an increase in the ratio of Gag to p25/p24 |
PubMed
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gag
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A single amino acid Phe676 of Alix is at the center of a large hydrophobic pocket and is crucial for binding to HIV-1 p6 |
PubMed
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gag
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Overexpression of AIP1(364-716) leads to a reduction in the cell-associated levels of HIV-1 Gag |
PubMed
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matrix
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gag
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In the absence of Vpu, Env accumulates extensively within clathrin-coated endosomal structures, including the viral proteins Gag and MA; the tetraspanins CD63 and CD81; the adaptor protein complex AP-3; and AIP1/ALIX, a cellular cofactor for viral budding |
PubMed
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nucleocapsid
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gag
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HIV-1 NC-mediated incorporation of ALIX into virions requires the zinc fingers of NC and the Bro1 domain of ALIX |
PubMed
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gag
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The N-terminal Bro1 domain (Brox) of ALIX bind to HIV-1 NC. Unexpectedly, Brox retains significant activity even if its CHMP4 binding site is disrupted |
PubMed
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gag
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Residues Q8, K11, K48, R51, R56, and K60 are part of the Bro1 domain of ALIX binding to HIV-1 NC, which involves RNA. Disruption of the Bro1-NC binding inhibits ALIX function in virus release |
PubMed
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gag
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The Bro1 domain of Alix inhibits HIV budding by targeting both PTAP/TSG101 and LYPXnL/Alix pathways. The NC domain of Gag is the primary target for Bro1 inhibition by Gag-mediated recruitment of Bro1 to the plasma membrane |
PubMed
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p6
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gag
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Knockdown of Alix by shRNA reduces the association of HIV-1 p6 with galectin-3 in cells |
PubMed
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gag
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A novel tetra-peptide insertion (PYXE), identified in Gag-p6 ALIX-binding region in protease inhibitor failure Indian HIV-1C sequences, may be predicted to restore ALIX-mediated virus release pathway |
PubMed
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gag
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The S40F mutation in HIV-1 p6 enhances ALIX binding to HIV-1 Gag in the yeast two-hybrid assay. The Y36S mutation introduced into the S40F mutant disrupts ALIX interaction with Gag and restores spherical particle formation in cells |
PubMed
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gag
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The phenolic hydroxyl of the tyrosine residue in the 36YPXnL domain of HIV-1 p6 is essential for ALIX-mediated HIV-1 budding. Y36F mutant blocks ALIX recruitment |
PubMed
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gag
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Mutations (Y36A, Y36S/L44H, Y36S/L44R, L41A, and L41R) between p6 residues 36 and 44 inhibit the Alix-p6 interaction |
PubMed
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gag
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AIP1 is incorporated into HIV-1 virions through its interaction with HIV-1 p6 |
PubMed
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gag
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AIP1 binds to the LXXLF motif in HIV-1 p6 (amino acids 41-44) and along with TSG101 acts as a component of the viral budding machinery |
PubMed
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gag
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Natural loss of L35Y36 residues in p6 of HIV-1 subtype C prevents p6 from ALIX interaction |
PubMed
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gag
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ALIX proteins with point mutations (Val498Asp, Phe676Asp, and Ile683Asp) that inhibit the p6 36YPLASL41 binding fail to rescue HIV-1 deltaPTAP release or infectivity |
PubMed
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gag
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An ALIX fragment encompassing residues 391-510 is a minimal p6deltaSQKQ binding site within the middle region of ALIX |
PubMed
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gag
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The Bro1 domain of Alix inhibits HIV budding by targeting both PTAP/TSG101 and LYPXnL/Alix pathways |
PubMed
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gag
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The ability of ALIX to rescue an HIV p6 PTAP mutant depends on its C-terminal proline-rich domain (PRD), but not on its binding sites for Tsg101 |
PubMed
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gag
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Overexpression of the Alix V domain inhibits HIV-1 release from cells; this inhibition of release is reversed by mutations that block binding of the Alix V domain to p6 |
PubMed
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gag
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Residues 360-702 of Alix spans the shape of the letter 'V' and is termed the V domain, which has a topologically complex arrangement of 11 alpha-helices; Phe676 is at the center of a large hydrophobic pocket and is crucial for binding to HIV-1 p6 |
PubMed
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