|
Envelope surface glycoprotein gp160, precursor
|
env
|
HIV-1 Vpu disrupts the co-localization between HIV-1 Env and tetherin in HeLa P4-R5 cells |
PubMed
|
|
env
|
BST-2 co-localizes with HIV-1 Env at the virological synapse on infected T cells |
PubMed
|
|
Nef
|
nef
|
HIV-1 group M Nef downregulates tetherin from the cell surface and is dependent upon amino acids at positions 4, 5, 28, 33, 40, 90, 103, and 109 in Nef |
PubMed
|
|
nef
|
HIV-1 (SF2) Nef downregulates BST2 (CD317/Tetherin); downregulation is dependent upon a proline-rich SH3 binding domain in Nef |
PubMed
|
|
nef
|
HIV-1 C1 Nef binds to residues in the N-terminus of human BST-2 (tetherin) and allows for HIV-1 release |
PubMed
|
|
nef
|
HIV-1 group M and O Nefs downregulate the longer isoform of human tetherin but not the shorter isoform |
PubMed
|
|
nef
|
Mutation of the four residues (K186V, Q188R, S192A, and L195T) in HIV-1 group O Nefs significantly reduces Nef-mediated downregulation of human tetherin |
PubMed
|
|
nef
|
HIV-1 group O Nefs evolve the ability to downregulate surface levels of tetherin and sequester it to intracellular perinuclear compartments |
PubMed
|
|
nef
|
Residues I163 and C169 of HIV-1 Nef from chimpanzee-adapted HIV-1 JC16 are specifically involved in its interaction with tetherin |
PubMed
|
|
nef
|
Tetherin upregulation in HIV-1-infected macrophages is HIV-1 Nef dependent, not a direct consequence of type I interferon induction |
PubMed
|
|
nef
|
HIV-1 replication in immature dendritic cells upregulates tetherin independently of Vpu, but in a Nef-dependent manner |
PubMed
|
|
Pr55(Gag)
|
gag
|
HIV-1 Vpu disrupts the co-localization between HIV-1 Gag and tetherin in a Trp-76-dependent manner in HeLa P4-R5 cells |
PubMed
|
|
gag
|
In cells expressing either wild-type or vpu(-) virus, BST-2 and HIV-1 Gag co-localize both along the plasma membrane and in endosomes |
PubMed
|
|
gag
|
BST-2 delays processing of cellular membrane-associated Gag proteins and adversely affects formation of the core structure in HIV-1 particles |
PubMed
|
|
gag
|
The interaction between HIV-1 Gag and TSG101 enhances tetherin recruitment in HeLa cells. Both TSG101 and ALIX binding sites within the p6 domain of Gag enhance tetherin recruitment to Gag assembly sites in T cells |
PubMed
|
|
gag
|
Tetherin potently inhibits release of Fyn(10)fullMA-Gag, which contains the first 10 amino acids of Fyn kinase at the N terminus of Gag, under cholesterol-depleting conditions in HeLa and HT-1080 cells |
PubMed
|
|
gag
|
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
|
|
gag
|
Tetherin accumulates with Gag at the contact zone between infected and target cells, but does not prevent the formation of virological synapses |
PubMed
|
|
gag
|
Cell-free virus particles produced from BST-2 and HIV-1(Vpu-) cotransfected 293T cells have a significant accumulation of the pr55Gag precursor and the p40Gag intermediate products, leading to diminish the infectivity of HIV-1 particles |
PubMed
|
|
Tat
|
tat
|
HIV-1 and the viral protein Tat modulate the expression of bone marrow stromal cell antigen 2 (BST2) in immature dendritic cells and monocyte-derived macrophages |
PubMed
|
|
Vpr
|
vpr
|
HIV-1 Vpr downregulates BST2 expression in human glial cells |
PubMed
|
|
Vpu
|
vpu
|
HIV-1 Vpu (membrane proximal basic residues required) increases the levels of a 23-kDa form of unglycosylated tetherin (transmembrane domain required) in the presence of overexpressed SGTA whereby the C-terminus of SGTA is required for this to occur |
PubMed
|
|
vpu
|
HIV-1 (NL4-3) Vpu downregulates BST2 (CD317/Tetherin); downregulation is dependent on the presence of serines at positions 52 and 56 in Vpu |
PubMed
|
|
vpu
|
HIV-1 subtypes A, B, C, D, and G Vpus inhibit tetherin and allow for HIV-1 release |
PubMed
|
|
vpu
|
HIV-1 Vpu antagonizes the effects of BCA2 on HIV-1 particle production in ""tetherin-positive"" cells |
PubMed
|
|
vpu
|
The betaTrCP binding motif DSGxxS of Vpu is required for optimal downregulation of BST-2 and enhancement of virion-release. Vpu serine (S52/S56) mutants are severely impaired for their ability to counteract tetherin antiviral activity |
PubMed
|
|
vpu
|
HIV-1 Vpus from transmission/founder virus clones downregulates BST2 (Tetherin) but do not efficiently downregulate CD4 |
PubMed
|
|
vpu
|
HIV-1 Vpu downregulates cell (CEMT4, Primary CD4+ T cells) surface expression of BST2 (tetherin) |
PubMed
|
|
vpu
|
Vpu counteracts BST2 (tetherin) antiviral activity in HIV-1 transduced cells (293T vs 293T stably expressing BST2(tetherin)) |
PubMed
|
|
vpu
|
Vpu from most transmission/founder HIV-1 downregulates BST2 and significantly correlates with level of virus release but did not efficiently downregulate CD4 |
PubMed
|
|
vpu
|
Vpu-mediated suppresion of IFN-1 production requires engagement and activation of the LILRA4 (ILT7) plasmacytoid dendritic cell receptor by BST2 |
PubMed
|
|
vpu
|
Vpu relocalizes/redistributes BST2 outside assembly sites in primary CD4+ T cells and in SupT1 cells expressing the short BST2 isoform |
PubMed
|
|
vpu
|
Vpu-mediated modulation of IFN-1 production by plasmacytoid dendritic cells requires the presence of BST2 on infected donor cells |
PubMed
|
|
vpu
|
HIV-1 Vpu antagonizes BST2 restiction of HIV-1 replication as demonstrated via mathematical modeling |
PubMed
|
|
vpu
|
HIV-1 (NL4-3) Vpu downregulates BST2 via a cullin-RING E3 ubiquitin ligase complex-independent mechanism |
PubMed
|
|
vpu
|
HIV-1 Vpu downregulates BST-2. The transmembrane/ion channel domain and conserved serines in the cytoplasmic domain of Vpu are required for the Vpu-mediated downregulation of BST-2 |
PubMed
|
|
vpu
|
HIV-1 Vpu counteracts the tetherin-induced retention of HIV-1(delVpu) virion particles. Vpu colocalizes with tetherin in co-expression cells |
PubMed
|
|
vpu
|
HIV-1 Vpu disrupts the co-localization between HIV-1 Gag and tetherin in a Trp-76-dependent manner in HeLa P4-R5 cells |
PubMed
|
|
vpu
|
HIV-1 Vpu interacts with BST-2 in the trans-Golgi network or in early endosomes, leading to lysosomal degradation of BST-2. Vpu-mediated downregulation of BST-2 depends on cellular ubiquitination machinery via betaTrCP |
PubMed
|
|
vpu
|
HIV-1 Vpu mutations (A19E, E29K, II43,46SL, R49G/T, SN53,55RH, S53N, E58K) derived from HIV-1 infected patients have defects for both CD4 and tetherin downregulation |
PubMed
|
|
vpu
|
HIV-1 Vpu stabilizes human tetherin in African green monkey kidney COS cells and still counteracts the ability of tetherin to suppress virus release |
PubMed
|
|
vpu
|
Expression of HIV-1 Vpu induces co-localization of tetherin with early endosome protein EEA-1 or late endosome protein LAMP-1 |
PubMed
|
|
vpu
|
The ability of HIV-1 Vpu to antagonize tetherin is important for the antibody opsonization of HIV-infected cells, which in turn increases FCGRIII (CD16) signaling |
PubMed
|
|
vpu
|
RNAi-knockdown of tetherin, but not CD4 or NTB-A, increases the resistance of HIV-infected cells to antibody-dependent cell-mediated cytotoxicity (ADCC), suggesting Vpu protects infected cells from ADCC as a function of its ability to counteract tetherin |
PubMed
|
|
vpu
|
N-terminally deleted BST-2 inhibits HIV-1 Vpu-defective and wild-type HIV-1 particle release, and the BST-2 mutant impairs its activity to activate NF-kappaB activation |
PubMed
|
|
vpu
|
The 59EXXXLV64 motif in HIV-1 Vpu is required for Vpu-mediated tetherin downregulation. Vpu E/L/V mutant fails to downregulate tetherin but still interact with beta-TrCP2 and HRS (ESCRT-0) |
PubMed
|
|
vpu
|
Vpu requires a functional polyubiquitin/proteasome system for efficient tetherin degradation. K48R ubiquitin mutant partially blocks Vpu-mediated tetherin downregulation |
PubMed
|
|
vpu
|
HIV-1 Vpu proteins from nonpandemic HIV-1 O and P strains are poor mediators of human tetherin downregulation. Vpus from nonpandemic HIV-1 N strains are as good tetherin antagonists as those from pandemic HIV-1 M strains |
PubMed
|
|
vpu
|
HIV-1 Vpu transmembrane mutants A14N and A18N do not support virus release in the presence of CD317, suggesting that Ala residues at position 14 and 18 are required to antagonize CD317 |
PubMed
|
|
vpu
|
Vpu interferes with tetherin trafficking to the cell-surface and causes a relocalization of the cellular tetherin with a TGN marker TGN46 in the TGN, suggesting Vpu-mediated antagonism of tetherin involves binding and sequestration of tetherin in the TGN |
PubMed
|
|
vpu
|
The plasma membrane clathrin adaptor protein complex AP-2 (mu2) is required for optimal downregulation of cell surface BST-2 by Vpu |
PubMed
|
|
vpu
|
All three major structural domains (amino-terminal cytoplasmic tail, transmembrane domain, and extracellular coiled-coil domain) of BST-2 are involved in Vpu-mediated antagonism of tetherin |
PubMed
|
|
vpu
|
The residues including 22 to 24 and 34 to 42 of tetherin play a crucial role in the Vpu interaction. I34, L37, and L41 of tetherin are involved in the determination of Vpu susceptibility |
PubMed
|
|
vpu
|
HIV-1 group N Vpu from Togo downregulates both tetherin isoforms. HIV-2 Env, SIVmac Nef, and KSHV K5 target tetherin isoforms with equal efficiency |
PubMed
|
|
vpu
|
Biotinylation technique in living cells demonstrates that HIV-1 Vpu-induced ER-to-cytosol retro-translocation of tetherin is first exposed to the cytosol as a dimeric oxidized complex and then becomes deglycosylated and reduces to monomers |
PubMed
|
|
vpu
|
Individual Vpu proteins isolated from chronically or acutely infected patients differ substantially in their CD4 and tetherin downregulation function at the cell surface |
PubMed
|
|
vpu
|
BiFC assay demonstrates that the cytoplasmic domain (CD) of HIV-1 Vpu physically interacts with both human and rhesus tetherins. The (G/D)DIWK motif in the CD of rhesus tetherin is responsible for the interaction and the functional antagonism by Vpu |
PubMed
|
|
vpu
|
HIV-1 Vpu-mediated BST-2 downregulation is critical for HIV-1 replication and propagation in vivo in a beta-TrCP dependent manner, especially at early times post-infection |
PubMed
|
|
vpu
|
The peptide BST2-TM-P1 competes with BST-2 binding to HIV-1 Vpu, resulting in restoration of the BST-2 level at HeLa-Vpu cell surface |
PubMed
|
|
vpu
|
Rhesus BST2 inhibits the release of HIV-1 from cells and is resistant to HIV-1 Vpu. Transfer of residues 30-45 of human BST2 into rhesus BST2 is sufficient to confer sensitivity to Vpu |
PubMed
|
|
vpu
|
HIV-1 Vpu interacts with CD317 via its transmembrane region (amino acids 4-27) in living cells |
PubMed
|
|
vpu
|
Alternative translation initiation produces two isoforms of tetherin, l-isoform and s-isoform, which restrict HIV-1 (Vpu-) particle release, but only l-isoform is sentitive to counteraction by Vpu |
PubMed
|
|
vpu
|
Human-monkey tetherin chimeras reveal that the transmembrane domains (amino acids I33V, I36L, P40L, and T45I) of tetherin are determinants of sensitivity/resistance to Vpu |
PubMed
|
|
vpu
|
The cytoplasmic tail of HIV-1 Vpu, specifically within the cytoplasmic tail hinge region (amino acids 47-60), are required for downregulation of both human tetherin and gibbon ape leukemia virus envelope (GaLV Env) |
PubMed
|
|
vpu
|
Chimeras between the TMD of HIV-1 M Vpu and the cytoplasmic domains of SIVcpzPtt, SIVcpzPts, and SIVgor Vpu proteins are capable of counteracting human tetherin to enhance virion release |
PubMed
|
|
vpu
|
The C-terminal alpha-helix (H2) of HIV-1 Vpu cytoplasmic tail domain (CTD) is sufficient to remove tetherin from sites of viral assembly and is necessary for full tetherin antagonist activity |
PubMed
|
|
vpu
|
The residues Q2, P3, I4, A7, V20, V21, V25, I26, and I27 of the TM domain in HIV-1 Vpu form crosslinks with the residues LLL22-4, G27, I28, L29, P40, L41, I43, F44, T45, and I46 of the TM domain in tetherin |
PubMed
|
|
vpu
|
Tetherin is in lipid rafts at the cell surface. Expression of HIV-1 Vpu relocalizes tetherin from the lipid rafts to intracellular endosome and lysosome compartments |
PubMed
|
|
vpu
|
Amino acid substitution variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations maintain its ability to restrict virion release but do not confer resistance to HIV-1 Vpu or SIVtan Env |
PubMed
|
|
vpu
|
HIV-1 Vpu proteins from Cameroonian group N viruses are largely unable to downregulate tetherin. Four amino acid substitutions (E15A, V19A and IV25/26LL) in the transmembrane domain of N-Vpu allow efficient interaction with human tetherin |
PubMed
|
|
vpu
|
HIV-1 Vpu inhibits endogenous expression BST2-induced NF-kappaB activity in cells, and the inhibition requires the beta-TrCP binding motif (residues 51-56; DSGxxS) in Vpu |
PubMed
|
|
vpu
|
HIV-1 Vpu variants from the group C show moderate virus release activity in comparison to group B Vpu variants. The TM domain from the inactive Vpu C is responsible for a significant decrease in egress activity and BST-2 downregulation |
PubMed
|
|
vpu
|
A combination of molecular dynamics simulations and docking approaches shows the lowest energy structure of Vpu-BST2, indicating that Leu-11/14/19/23 and Ile-10/15/18 in BST2 interact with the alanine rim (Ala-8/11/15/19) of Vpu |
PubMed
|
|
vpu
|
Analysis of the chimera HIV-1 Vpu proteins from group M and O shows that alanine-18 is important for group M Vpu localization and tetherin-Vpu interaction |
PubMed
|
|
vpu
|
Overexpression of BST2 and downregulation of HIV-1 Vpu in HIV-1 infected TZM-bl cells inhibit HIV-1 replication |
PubMed
|
|
vpu
|
The retention of HIV-1 Vpu from group O in ER-associated compartments confers a defect to antagonism even when interaction with tetherin is mediated through a chimeric TM domain |
PubMed
|
|
vpu
|
Tetherin delGPI mutant directly interacts with HIV-1 Vpu and inhibits Vpu-induced degradation of tetherin and CD4. Transient expression of tetherin delGPI mutant also inhibits infectious HIV-1 release in tetherin-positive cells |
PubMed
|
|
vpu
|
HIV-1 Vpu downregulates cell-surface BST-2 levels without qualitatively affecting the distribution of the restriction factor at the plasma membrane in HIV-1-infected Jurkat cells |
PubMed
|
|
vpu
|
SCYL2 inhibits Vpu-induced BST2 and CD4 reduction at the cell surface by suppressing the phosphorylation of Vpu at positions Ser-52 and Ser-56 |
PubMed
|
|
vpu
|
HIV-1 Vpu from chimpanzee-adapted HIV-1 JC16 downregulates both human and chimpanzee tetherin proteins as efficiently as that of HIV-1 NL4-3 Vpu |
PubMed
|
|
vpu
|
Alanine-scanning mutagenesis and Ala-to-Leu replacement through the HIV-1 Vpu transmembrane domain (residues 5-28) reveals A14 and W22 are required for tetherin antagonism |
PubMed
|
|
vpu
|
HIV-1 BF recombinant Vpu is associated with increased viral particle production when compared to WT B variant virus in tetherin-expressing cell lines |
PubMed
|
|
vpu
|
HIV-1 Vpu rescues the decreased production of infectious HIV-1 virions and restores the diminished reverse transcriptase activities of the culture supernatants as a result of BST-2 inhibition |
PubMed
|
|
vpu
|
Lysine residues (K18/K21) in tetherin are determinants for Vpu-mediated depletion of tetherin. This depletion, however, is dispenable for potent antagonism of the tetherin-mediated restriction of HIV-1 particle release |
PubMed
|
|
vpu
|
A functional ER-associated degradation pathway is required for Vpu-induced tetherin degradation. P97 ATPase (VCP) knockdown partially impairs Vpu-mediated tetherin degradation |
PubMed
|
|
vpu
|
Tetherin cytoplasmic tail lysine residues (K18 and K21) are ubiquitinated in the presence of HIV-1 Vpu and KSHV K5 |
PubMed
|
|
vpu
|
HIV-1 Vpu transmembrane domain mutants V9D and I19D fail to promote HIV-1 virion release and to downregulate cell surface tetherin |
PubMed
|
|
vpu
|
Mutation of a single amino acid (T45I) in the transmembrane region of BST-2 results in insensitivity to HIV-1 Vpu while maintaining antiviral activity |
PubMed
|
|
vpu
|
HIV-1 Vpu co-immunoprecipitates with BST-2 in HEK293T cells and in HeLa Tet-Off cells. Deletion of two leucine residues at positions 22 and 23 in tetherin diminishes its association with Vpu |
PubMed
|
|
vpu
|
HIV-1 Vpu reduces steady-state expression of BST-2 in transfected HeLa cells and in HIV-infected macrophages, but not in HIV-infected CEMx174 and H9 cells |
PubMed
|
|
vpu
|
HIV-1 Vpu-A18H downregulates the expression of BST-2 at the cell surface and enhances virion release inefficiently through a reduced interaction with BST-2 |
PubMed
|
|
vpu
|
Tetherin inhibits influenza virus neuraminidase (NA) virus-like particle (VLP) release, which is antagonized by HIV-1 Vpu |
PubMed
|
|
vpu
|
In HIV-1-producing cells, CD317 relocalizes predominantly to TfR-positive recycling endosomes, to EEA1-postive early endosomes, and to gin97-positive trans-Golgi network compartments, with some present on late endocytic structures |
PubMed
|
|
vpu
|
All potential acceptor sites (Ser3, Thr4, Ser5, Cys9, Lys18, Cys20, and Lys21) in the cytoplasmic domain of BST2 contribute to Vpu-induced ubiquitination |
PubMed
|
|
vpu
|
BIT225, HIV-1 Vpu viroporin inhibitor, does not affect Vpu-tetherin interactions |
PubMed
|
|
vpu
|
Reduced HIV-1 release in Rab7A-depleted cells is related to expression of the restriction factor tetherin, suggesting that Rab7A contributes to the mechanism by which Vpu counteracts tetherin and rescues HIV-1 release |
PubMed
|
|
vpu
|
SHIV Vpu proteins can counteract human and rhesus BST-2 |
PubMed
|
|
vpu
|
A computer modeling method predicts that the interface is composed of Vpu residues I6, A10, A14, A18, V25 and W22, and BST-2 residues L23, I26, V30, I34, V35, L41, I42, and T45 |
PubMed
|
|
vpu
|
Endogenous tetherin cell surface expression in T-cell lines H9, CEM-CCRF and CEM-SS are different and that affects HIV-1 Vpu-mediated tetherin modulation on virus release |
PubMed
|
|
vpu
|
An N-terminal deletion and T45I substitution in the TMD of human tetherin render the protein unresponsive to antagonism by HIV-1 Vpu |
PubMed
|
|
vpu
|
NMR studies reveal that the 10AXXXAXXXAXXXW22 face of the Vpu transmembrane domain (TMD) directly binds to the large hydrophobic residues (aa 22-47) of the tetherin TMD in an anti-parallel manner |
PubMed
|
|
vpu
|
The C-terminal fragment of the clathrin assembly protein AP180 inhibits the downregulation of BST-2 from the cell surface by HIV-1 Vpu and HIV-2 Env |
PubMed
|
|
vpu
|
Dominant negative dynamin 2 (K44A) acts as an inhibitor of clathrin-mediated endocytosis and that it inhibits the downregulation of BST-2 from the cell surface by HIV-1 Vpu and HIV-2 Env |
PubMed
|
|
vpu
|
The putative cholesterol recognition amino acid consensus (CRAC) motif (residues 25-31) of HIV-1 Vpu mediates lipid raft association of Vpu, but is dispensable for the downregulation of cell surface BST-2 |
PubMed
|
|
vpu
|
Tetherin expression is upregulated following HIV-1 infection of monocytes-derived macrophages and is not fully downregulated by HIV-1 Vpu |
PubMed
|
|
vpu
|
HIV-1 Vpu partially antagonizes the restriction of BST2 on HCV production and release from BST2 expressing Huh7.5 cells |
PubMed
|
|
vpu
|
Downregulation of CD4 and BST2 by HIV-1 Vpu is observed in HIV-1 infected humanized mice |
PubMed
|
|
vpu
|
P40L/T45I mutations in human tetherin leads to drastically decreased susceptibility of the mutant to HIV-1 Vpu, while susceptibility to SIVden Vpu increases to 50%, suggesting that these two residues participate in the species-specific activity of Vpu |
PubMed
|
|
vpu
|
Overexpression of clathrin coat-associated protein AP180 inhibits Vpu-mediated tetherin antagonism but adaptor protein-1, adaptor protein-2, and adaptor protein-3 are dispensable |
PubMed
|
|
vpu
|
HIV-1 Vpu E/L/V mutants interact with tetherin in infected cells and are incorporated into nascent virions in a tetherin-dependent manner |
PubMed
|
|
vpu
|
Mutation of the 59EXXXLV64 motif in HIV-1 Vpu leads to endosomal and surface localization of Vpu and modulates the trafficking of tetherin |
PubMed
|
|
vpu
|
The ubiquitin associated protein 1 (UBAP1)-containing ESCRT-I is essential for degradation of antiviral cell-surface protein such as tetherin (BST-2/CD317) by HIV-1 Vpu |
PubMed
|
|
vpu
|
IFNalpha/ribavirin treatment in vivo induces APOBEC3G, APOBEC3F, and BST-2 expression and results in hyper-mutations in viral genome and A11G/S61A mutations in HIV-1 Vpu. These two mutations in Vpu enhances the interaction between BST-2 and Vpu |
PubMed
|
|
vpu
|
Cholesterol-binding compound amphotericin B methyl ester (AME) inhibits the ability of HIV-1 Vpu to counteract the activity of CD317/BST-2/tetherin |
PubMed
|
|
vpu
|
Deletion of amino acids leucine's 22/23 in BST-2 significantly diminishes its association with Vpu, leading to its resistance to antagonism by Vpu |
PubMed
|
|
vpu
|
Monomeric tetherin and non-glycosylated tetherin are expressed at the cell surface and are sensitive to Vpu-induced downregulation |
PubMed
|
|
vpu
|
HIV-1 Vpu and beta-TrCP co-immunoprecipitate with tetherin |
PubMed
|
|
vpu
|
The v-ATPase VPS4 is required for Vpu-induced cell surface downregulation of BST-2 |
PubMed
|
|
vpu
|
HRS interacts with both HIV-1 Vpu and tetherin by co-precipitation analysis |
PubMed
|
|
vpu
|
HRS, an ESCRT-0 complex component, is required for the Vpu-induced downregulation of BST-2, indicating that Vpu-induced BST-2 degradation involves the ESCRT/MVB pathway |
PubMed
|
|
vpu
|
Co-depletion of beta-TrCP1 and beta-TrCP2 support Vpu's activity to enhance virus release and to downregulate endogenous tetherin in TZM-bl cells |
PubMed
|
|
vpu
|
The STS sequence in the cytoplasmic domain of BST2 is required for optimal Vpu-mediated downregulation of BST2 from the cell surface and the counteraction of virion release by Vpu |
PubMed
|
|
vpu
|
HIV-1 Vpu accelerates the turnover of mature endogenous BST-2 in both HeLa and CEMx174 cells. The interference of Vpu with the newly synthesized BST-2 results in the gradual depletion of cell surface BST-2 |
PubMed
|
|
vpu
|
CD317 exhibits a fast recycling kinetic that is sensitive to treatment with primaquine, a strong recycling inhibitor. HIV-1 Vpu interferes with the recycling of CD317 |
PubMed
|
|
vpu
|
HIV-1 Vpu ion channel mutant S23A binds and antagonizes CD317, indicating that its ion channel function is not correlated with its ability to downregulate cell surface CD317 |
PubMed
|
|
vpu
|
HIV-1 Vpu cytoplasmic domain mutants S56G and E59K fail to enhance HIV-1 virion release but can reduce cell surface tetherin, suggesting that downregulation of cell surface tetherin and enhancement of virion release by Vpu are not always correlated |
PubMed
|
|
capsid
|
gag
|
HIV-1 CA mutations, P99A and EE75,76AA, pair in tetherin recruitment to HIV-1 assembly sites |
PubMed
|