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Pr55(Gag)
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gag
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A3H hapI-GKE and hapII-RDD variants are packaged into virions through an association with the matrix-capsid region (amino acids 10-277) and with the NC region (amino acids 378-432) of Gag in an RNA-dependent manner, respectively |
PubMed
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Vif
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vif
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The combination of N48H and GDAK60-63EKGE results in a hyperfunctional Vif protein capable of fully inhibiting stable APOBEC3H-hapII |
PubMed
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vif
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Single mutations I31V, R33G, K36R, and K50R in HIV-1 Vif from NL4-3 sufficiently reduce or abolish their ability to cause G2 arrest, but induce APOBEC3H degradation |
PubMed
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vif
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HIV-1 Vif proteins from NL4-3, SG3, and C2 have the ability to induce G2 arrest in HEK293T cells, but are defective in inducing APOBEC3H degradation when compared to HIV-1 Vif from HXB2 |
PubMed
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vif
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A3H interacts with both HIV-1 Vif(IIIB) and Vif(HXB2) in cells and in vitro, but Vif(IIIB) fails to degrade A3H and Vif(HXB2) H48N mutant reduces its ability to degrade A3H in cells |
PubMed
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vif
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A histidine at position 48 (48H) in HIV-1 Vif confers activity against A3H-hapII, while an asparagine (48N) abolishes its anti-A3H activity |
PubMed
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vif
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A glutamic acid at position 121 (121E) renders A3H-hapII sensitivity to both LAI and NL4-3 Vif proteins, while a lysine (121K) results in resistance of A3H-hapII to both Vif alleles |
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
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vif
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APOBEC3H variants encoding a SNP cluster (G105R, K121D and E178D, hapII-RDD) restrict human immunodeficiency virus type 1 (HIV-1) more efficiently than wild-type APOBEC3H (hapI-GKE). All APOBEC3H variants are resistant to HIV-1 Vif |
PubMed
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vif
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Once expression is optimized and stabilized, human A3H can significantly reduce HIV-1 infectivity. HIV-1 Vif fails to suppress A3H activity |
PubMed
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vif
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The interaction of HIV-1 Vif(HXB2) with A3H induces polyubiquitination of A3H at K63 position |
PubMed
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vif
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HIV-1 Vif variants from subtype F are highly effective in counteracting A3H hapII. Two residues in the amino-terminal region of Vif (positions 39F and 48H) from HIV-1 subtype F are necessary for association of Vif with A3H hapII |
PubMed
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vif
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HIV-1 Vif 39F efficiently inhibits A3H-hapII, but Vif 39V is defective in counteracting A3H-hapII. Mutation at position 39F to the different residues (C, E, G, H, I, K, L, S, T, and V) is inactive against A3H-hapII, but only 39Y can counteract A3H-hapII |
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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G105R and K121E residues are important for A3H (HapI) stability and increased antiviral activity and for the resistance of A3H (HapI) to Vif, respectively |
PubMed
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vif
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HIV-1 Vif targets A3H (HapII) for proteasome-mediated degradation. L64, I66, Y69, and L72 residues in Vif are required for Vif-mediated A3H degradation |
PubMed
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nucleocapsid
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gag
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A3H (HapVII) virion packaging is dependent on a (112)YYXW(115) motif, which binds HIV-1 nucleocapsid in an RNA-dependent manner. A single Y112A mutation completely disrupts A3H virion incorporation |
PubMed
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