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Envelope surface glycoprotein gp120
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env
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CD63 enhances HIV-1 gp120/gp41-mediated entry in human macrophages |
PubMed
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env
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HIV-1 Gag, CA, and gp120 proteins co-localizes with CD63 and acetylcholinesterase (ACHE)-associated exosomes from supernatants of HIV-1 expressing cells. The 5' end of the Gag p17 open reading frame is sufficient for HIV-1 RNA exosome incorporation |
PubMed
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env
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Recruitment of Env to tetraspanin-enriched micro domains (TEMs) is required for cell-cell fusion repression by CD9 and CD63 |
PubMed
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env
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Tetraspanin proteins, such as CD9, CD63, CD81, CD82, and CD231, are incorporated on the membrane of released virions in an HIV-1 envelope protein (Env)-independent manner and have the potential to inhibit HIV-1 Env-mediated infection |
PubMed
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Envelope surface glycoprotein gp160, precursor
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env
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HIV-1 Env co-localizes with CD63 in HIV-1 infected CD4+ T cells |
PubMed
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env
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Recruitment of Env to tetraspanin-enriched micro domains (TEMs) is required for cell-cell fusion repression by CD9 and CD63 |
PubMed
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env
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DLG1 knockdown is associated with the redistribution and colocalization of Env toward CD63 and CD82 positive vesicle-like structures |
PubMed
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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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env
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CD63 localizes to endosome compartments and is incorporated into the viral envelope of macrophage-derived HIV-1 particles |
PubMed
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Envelope transmembrane glycoprotein gp41
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env
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HIV-1 gp41 co-localizes predominantly with CD63 at the virological synapse of Jurkat cells |
PubMed
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env
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CD63 enhances HIV-1 gp120/gp41-mediated entry in human macrophages |
PubMed
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env
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Recruitment of Env to tetraspanin-enriched microdomains (TEMs) is required for cell-cell fusion repression by CD9 and CD63 |
PubMed
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env
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Tetraspanin proteins, such as CD9, CD63, CD81, CD82, and CD231, are incorporated on the membrane of released virions in an HIV-1 envelope protein (Env)-independent manner and have the potential to inhibit HIV-1 Env-mediated infection |
PubMed
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Nef
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nef
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HIV-1 Nef induces release of CD63 (MAL-dependent exosome marker) from Jurkat T cells transfected with DNA constructs coding for Nef-GFP |
PubMed
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nef
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Both HIV-1 Nef and Vpu downregulate the cell surface expression of CD63 (TSPAN30) |
PubMed
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nef
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HIV-1 Nef targets CD4 to CD63-containing lysosomes for Nef-induced degradation of CD4, which requires the VPS4-mediated ESCRT machinery |
PubMed
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nef
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HIV-1 Nef increases the production of exosomes, which form in the late endosomes and co-localizes with the late endosomal marker CD63 in SupT cells |
PubMed
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nef
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HIV-1 Nef increases the production of exosomes, 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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Co-localization of HIV-1 Gag virus-like particles in THP-1/CD169YF cells is reduced within CD81+ compartments, but enhanced within CD63+ or LAMP1+ compartments |
PubMed
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gag
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HIV-1 Gag proteins co-localize with CD63 and CD81 in intracellular exosomes |
PubMed
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gag
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HIV-1 Gag, CA, and gp120 proteins co-localizes with CD63 and acetylcholinesterase (ACHE)-associated exosomes from supernatants of HIV-1 expressing cells. The 5' end of the Gag p17 open reading frame is sufficient for HIV-1 RNA exosome incorporation |
PubMed
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gag
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Tetherin co-localizes with HIV-1 Gag in CD81- and CD63-enriched intracellular virus-containing compartments in macrophages, and that a separate population of tetherin is located in the TGN |
PubMed
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gag
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The budding defect of p6-deficient HIV-1 Gag is caused primarily by C-terminal exposure of p1. The p1 domain of p6-deficient Gag acts as an inhibitory budding signal by blocking the interaction of Gag with CD63 and VPS4B |
PubMed
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gag
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Env-mediated cell-cell fusion repression by CD9 and CD63 requires the presence of HIV-1 Gag |
PubMed
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gag
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DLG1 knockdown is associated with the redistribution and colocalization of Gag toward CD63 and CD82 positive vesicle-like structures |
PubMed
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gag
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HIV-1 Gag proteins co-localize with tetraspanins CD9, CD81, and CD82 in CD63-enriched micro domains |
PubMed
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gag
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A dileucine-like motif (residues 321-322) in HIV-1 Gag regulates the assembly of Gag into CD63-positive multivesicular bodies |
PubMed
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gag
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In human macrophages, HIV-1 Gag proteins co-localize with MHC II (HLA-DR), CD63, and Lamp1 in MHC II compartments |
PubMed
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Tat
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tat
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siRNA-mediated CD63 down regulation reduces production of the early HIV protein Tat in both macrophages and a CD4(+) cell line |
PubMed
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Vpu
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vpu
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Both HIV-1 Nef and Vpu downregulate the cell surface expression of CD63 (TSPAN30) |
PubMed
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capsid
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gag
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HIV-1 Gag colocalizes with CD63 in U1/HIV-1 cells (chronically infected monocytoid cells harboring 2 integrated copies of HIV provirus per cell) |
PubMed
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gag
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siRNA knockdown of CD63 in U1/HIV-1 cells (chronically infected monocytoid cells harboring 2 integrated copies of HIV provirus per cell) affects CA (p24) levels in supernatants (decreases) but not intracellular CA (p24) levels |
PubMed
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gag
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HIV-1 Gag, CA, and gp120 proteins co-localizes with CD63 and acetylcholinesterase (ACHE)-associated exosomes from supernatants of HIV-1 expressing cells. The 5' end of the Gag p17 open reading frame is sufficient for HIV-1 RNA exosome incorporation |
PubMed
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gag
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CD63 silencing inhibits production of the late protein CA p24 in early HIV-1 replication events in both macrophages and a CD4(+) cell line |
PubMed
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gag
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In human macrophages, HIV-1 Capsid (p24) co-localizes with MHC II (HLA-DR), CD63, and Lamp1 in MHC II compartments |
PubMed
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matrix
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gag
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HIV-1 Gag colocalizes with CD63 in U1/HIV-1 cells (chronically infected monocytoid cells harboring 2 integrated copies of HIV provirus per cell) |
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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