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Envelope surface glycoprotein gp120
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env
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HIV-1 Env gp120 variable loop 3 (V3) region mutation is increased by incomplete Vif neutralization (Vif K22E) of APOBEC3G/F activity and may contribute to genetic evolution from CCR5 to CXCR4 co-receptor usage |
PubMed
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Pol
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gag-pol
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Analyses of longitudinal HIV-1 pol sequences from patients without hypermutated viruses during chronic infection indicate that A3F may increase HIV-1 diversification and facilitate viral adaption and propagation in vivo |
PubMed
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Pr55(Gag)
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gag
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R7R10K11S, A30P, P31L, R32G, and RKK32-34SSS mutations in the NC domain of HIV-1 Gag result in a significant decrease in APOBEC3F incorporation into virus-like particles |
PubMed
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gag
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Amino acids 104-156, located between the two cytidine deaminase domains of APOBEC3F, are required for its incorporation into Gag virus-like particles |
PubMed
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gag
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The NC domain of HIV-1 Gag is required for 7SL RNA and APOBEC3F packaging |
PubMed
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|
gag
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APOBEC3F may be incorporated into virions by HIV-1 Gag polyprotein |
PubMed
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gag
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Single-virion fluorescence microscopy analysis demonstrates that the efficiency of A3G-YFP and A3F-YFP incorporation into HIV-1 Gag-CeFP virions is higher than that of A3C-YFP incorporation into HIV-1 Gag-CeFP virions |
PubMed
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gag
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The efficiency of incorporation of Mov10, A3G, and A3F into viral particles, which contains both HIV-1 Gag and genomic RNA, is much higher than that of the other P-body proteins AGO2, DCP1a, DCP2, and DDX6 |
PubMed
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gag
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In HIV-1 virions, APOBEC3F interacts with HIV-1 IN and NC, which are known to be important for reverse transcription and integration |
PubMed
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Vif
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vif
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HIV-1 Vif binds APOBEC3F; the interaction is between amino acid residue R15 in Vif and E289 in APOBEC3F |
PubMed
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vif
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HIV-1 Vif degrades APOBEC3F; degradation is dependent on interactions between amino acid residue R15 in Vif and E289 in APOBEC3F |
PubMed
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vif
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HIV-1 Vif degrades APOBEC3F dependent upon L291, A292, R293, and E324 in APOBEC3F |
PubMed
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|
vif
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HIV-1 Vif binds amino acids L291, A292 and R293 in APOBEC3F |
PubMed
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vif
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HIV-1 Vif degrades APOBEC3C and APOBEC3F and is dependent on Vif F1, F2, and F3 box mutations involving residues D14, R15, M16, W79, D172, and W174 |
PubMed
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vif
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HIV-1 Vif degrades APOBEC3F and APOBEC3C |
PubMed
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vif
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HIV-1 Vif internal amino acid salt bridge (E171-K167-D101) mediates human APOBEC3C and APOBEC3F degradation |
PubMed
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vif
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HIV-1 Vif specifically binds APOBEC3F, and Vif suppresses both the inhibition of virus infectivity caused by APOBEC3F and virion incorporation of APOBEC3F |
PubMed
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vif
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APOBEC3F levels are increased by compound N.41 treatment only in cells co-expressing HIV-1 Vif, and APOBEC3F levels in virus particles are also increased |
PubMed
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|
vif
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APOBEC3F, similar to APOBEC3G, induces G to A hypermutations in HIV-1 genomic DNA, and the HIV-1 Vif protein inhibits this activity |
PubMed
|
|
vif
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Certain residues L125, G126, R127, E134, Y135, G138 in HCCH motif (residues 125-141) of HIV-1 Vif are required for inhibition of APOBEC3F |
PubMed
|
|
vif
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Immunoblotting and crystal structure analyses reveal ten amino acids L225, F258, C259, I262, L263, S264, Y269, D289, F290, and H294 in APOBEC3F are involved in forming Vif-interaction interface |
PubMed
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vif
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A potent small molecular compound VEC-5 protects APOBEC3G, APOBEC3F, and APOBEC3C from HIV-1 Vif-induced degradation and enhances A3G incorporation into HIV-1 virions by inhibiting the interaction between Vif and elongin C |
PubMed
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vif
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HIV-1 Vif W21A, S32A, W38A, Y69A, E76A, W79A, H108A, C114S, C133S, and H139A mutants have no viral ability to neutralize APOBEC3F |
PubMed
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vif
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An extensive mutational analysis of HIV-1 Vif reveals that two distinct regions of Vif, amino acids Y(40)RHHY(44) and D(14)RMR(17), which are essential for binding to A3G and A3F, respectively |
PubMed
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vif
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CBF-beta-mediated increase of HIV-1 Vif steady-state levels results in decreased cellular levels of all Vif-sensitive APOBEC proteins (A3C, A3D, A3F, A3G, and A3H haplotype II) |
PubMed
|
|
vif
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Endogenous APOBEC3 proteins, particularly APOBEC3D, APOBEC3F, and APOBEC3G, can potently inhibit HIV-1 propagation in a mouse model by mutating 14DRMR17 and/or 40YRHHY44 motifs in Vif |
PubMed
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vif
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Amino acids P281, E282, D313, E316, Q323, and E324 in APOBEC3F are required for the interface binding to HIV-1 Vif(IIIB) |
PubMed
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vif
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HIV-1 Vif mutants 84DVAAAA89, 88EW/AA89, G84A, G84D, W89A, D104A, L106S, and I107S result in upregulated APOBEC3F expression and show a reduced ability to neutralize the antiviral activity of APOBEC3F |
PubMed
|
|
vif
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HIV-1 Vif mutant E88A/W89A fails to bind to CBF-beta, which impairs Vif-mediated degradation of both A3F and A3G proteins and HIV-1 replication in non-permissive CEM cells |
PubMed
|
|
vif
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A novel conserved 69YXXL72 motif in HIV-1 Vif mediates binding to human A3F and its subsequent degradation. Tyr69 and Leu72 residues in the YXXL motif are important for degradation of A3F |
PubMed
|
|
vif
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HIV-1 Vif, which suppresses both APOBEC3G and APOBEC3F antiviral function by inducing their degradation, may selectively remove these proteins from, and/or restrict their localization to, P-bodies |
PubMed
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|
vif
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HIV-1 Vif mutants W11R and R15G are restricted in permissive SupT11 and nonpermissive CEM2n cell lines that express A3F, while H43N and H43N/E117K Vif mutants are capable of spreading efficiently in the presence of A3F |
PubMed
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vif
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HIV-1 Vif mutants W5S, W21S, W38S, W89S, F112S, and F115S have a reduced ability to interact with CBF-beta and these Vif hydrophobic residues are important for Vif-mediated degradation of A3F |
PubMed
|
|
vif
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The crystal structure provides a structural basis that L255A, L255D, F258A, C259K, C259S, I262A, Y269A, E286A, E289Q, F290A, F290K, H294A, H294D, E316Q, S320A, and E324Q mutations fail to bind to HIV-1 Vif |
PubMed
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|
vif
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The HIV-1 Vif N-terminal motif (residues 18-38) binds CUL5 in mammalian cells and is reguired for A3F and A3G degradation and HIV-1 infectivity |
PubMed
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|
vif
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Replacement of all lysines with arginines in A3F results in inhibition of HIV-1 Vif-mediated A3F degradation by polyubiquitination. Lysines at positions 40, 52, 209, 334, 337, 355, and 358 in A3F are important for its degradation by Vif |
PubMed
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vif
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A3F mutants C259K and IL262-263AA are resistant to HIV-1 Vif-mediated A3F degradation |
PubMed
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|
vif
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The amino acids 223-232 of A3F-CTD beta1-2 loop is conserved to the amino acids 23-32 of HIV-1 Vif, while the amino acids 305-313 of A3F-CTD beta4-alpha4 loop is conserved to the amino acids 108-113 of HIV-1 Vif |
PubMed
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|
vif
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Unusual substitutions V13I, V55T, and L81M in HIV-1 Vif from children infected perinatally without progression to AIDS are located in three distinct Vif motifs important for the interaction with A3G/A3F |
PubMed
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|
vif
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The antiviral activity of A3G to HIV-1 vif mutants NL4-3 40YRHHY44>A5 and NL4-3 14DRMR17>A4 with G-to-A hypermutations confers a greater restriction than the combined antiviral activity of A3F and A3DE in activated CD4+ T cells and macrophages |
PubMed
|
|
vif
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HIV-1 Vif alleles from seven HIV-1 subtypes show their abilities to degrade and counteract A3F efficiently |
PubMed
|
|
vif
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Highly conserved Tryptophan residues in the N-terminal region of HIV-1 Vif are required for the suppression of both APOBEC3G and APOBEC3F |
PubMed
|
|
vif
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HIV-1 Vif motif TGERxW (amino acids 74-79) is important for A3F interaction and inhibition |
PubMed
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vif
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Stress causes A3A, A3B, A3C, and A3F to co-localize efficiently with Vif(IIIB) and mRNA-PABP1 complexes in stress granules |
PubMed
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vif
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Vif-deficient HIV-1 replicates as equally well as wild-type virus in CEM-T4 cells expressing high levels of A3G and A3F, indicating CEM-T4 cells lack a cellular co-factor for these endogenous antiretroviral proteins |
PubMed
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vif
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Small molecule RN-18 specifically inhibits HIV-1 Vif-mediated downregulation of APOBEC3C/F/G proteins by decreasing Vif protein levels when Vif interacts with these proteins |
PubMed
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|
vif
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Amino acids 283 to 300 of A3F are critical for binding to the DRMR region of HIV-1 Vif and for A3F degradation |
PubMed
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|
vif
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The SLV portion of the Vif SLV/Ix4Yx9Y motif is required for optimal suppression of A3F |
PubMed
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|
vif
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The carboxyl-terminal domain (residues 183-373) of A3F alone binds to HIV-1 Vif and behaves like the full-length A3F in terms of Vif sensitivity |
PubMed
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vif
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Human T cell line CEM.NKR clones display inhibition of HIV-1 replication although these clones retain low levels of A3DE, A3F, A3G, and A3H expression, suggesting that a novel restriction factor distinct from APOBEC3s exists in CEM.NKR cells |
PubMed
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vif
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Incorporation of Vif into virions is dependent on its interaction with A3G/A3F |
PubMed
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|
vif
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Long-term restriction by A3F selects HIV-1 clones with Vif Q26-Q27 or Y26-Q27 mutations, which are fully capable of overcoming A3F but susceptible to restriction by A3G |
PubMed
|
|
vif
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Alternative splice removal of exon 2 of A3F produces a Vif-resistant protein that retains significant antiviral activity. Splice removal of exons 2-4 results in a Vif-sensitive A3F protein with weaker antiviral activity |
PubMed
|
|
vif
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The T(Q/D/E)x(5)ADx(2)(I/L) motif, located at residues 96 to 107 in HIV-1 Vif, plays a critical role in neutralizing activity toward A3F. This motif regulates Vif interaction with Cul5 |
PubMed
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|
vif
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All residues except N175 in the (171)EDRWN(175) domain of Vif are equally important for regulation of A3F neutralization |
PubMed
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|
vif
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Residues L81, G82, and G84, and, to a lesser extent, I87 and W89 within the (81)LGxGxxIxW(89) domain affect Vif binding to A3F and play very critical roles in A3F neutralizing activity |
PubMed
|
|
vif
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Amino-acid residues QE323-324EK in A3F affect the differential susceptibility of human A3F and monkey A3F to HIV-1 Vif. Mutation of A3F E324 alone alters functional susceptibility of its binding to Vif |
PubMed
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|
vif
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Amino acid E289 in the EFLARH sequence of A3F is critical for HIV-1 Vif sensitivity |
PubMed
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|
Vpu
|
vpu
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The expression of APOBEC3F is enhanced in Vpu-deficient HIV-1-infected cells as compared to that in wild-type-infected cells |
PubMed
|
|
capsid
|
gag
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HIV-1 CA mutations (K203A and E128A/R132A) that alter HIV-1 core stability decrease nuclear import of A3F-YFP-labeled preintegration complexes (PICs) in infected cells |
PubMed
|
|
integrase
|
gag-pol
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In HIV-1 virions, APOBEC3F interacts with HIV-1 IN and NC, which are known to be important for reverse transcription and integration |
PubMed
|
|
nucleocapsid
|
gag
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The NC domain of HIV-1 Gag is required for 7SL RNA and APOBEC3F packaging |
PubMed
|
|
gag
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In HIV-1 virions, APOBEC3F interacts with HIV-1 IN and NC, which are known to be important for reverse transcription and integration |
PubMed
|
|
reverse transcriptase
|
gag-pol
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Vif-negative HIV-1 produced from 293T cells transiently expressing hA3F is impaired in early and late viral DNA production, and in viral infectivity, effects that are correlated with an inability of tRNA(3)(Lys) to prime reverse transcription |
PubMed
|
|
gag-pol
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APOBEC3-driven mutagenesis contributes to the generation of both M184I and E138K mutations in HIV-1 RT in the absence of drug exposure |
PubMed
|