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Pr55(Gag)
|
gag
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The viruses expressing Gag proteins from clinical isolates show differences in their sensitivity to TRIM5alpha, which is dependent on the TRIM5alpha alleles that the virus encounters |
PubMed
|
|
Tat
|
tat
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Overexpression of HIV-1 Tat results in a nonspecific activation of the expression of TRIM5alpha |
PubMed
|
|
Vpu
|
vpu
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The expression of TRIM5 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 infection is modestly restricted by human TRIM5alpha, which acts on the incoming HIV-1 capsid |
PubMed
|
|
gag
|
Removal of a positively charged residue at position 332 of human TRIM5alpha increases its restricting activity by increasing the ability of TRIM5alpha to bind HIV-1 capsid complexes |
PubMed
|
|
gag
|
Intra- and inter-hexamer crosslinking demonstrate the interaction between HIV-1 CA and human TRIM5alpha CC-SPRY domains (residues 132-493) |
PubMed
|
|
gag
|
HIV-1 CA residues 83, 89, 120, 122 and the aromatic residues 117, 130, and 133 modulate its sensitivity to TRIM5alpha |
PubMed
|
|
gag
|
TRIM5alpha disrupts the regular cylindrical hexameric lattice structure of HIV-1 CA-NC complex |
PubMed
|
|
gag
|
HIV-1 capsid is more rapidly degraded in cells expressing monkey TRIM5alpha than in cells expressing human TRIM5alpha |
PubMed
|
|
gag
|
R332G/R335G and R330E/R332G/R335G mutants of TRIM5alpha binds the in vitro-assembled CA-NC complexes and the strength of the interaction correlates with the magnitude of restriction |
PubMed
|
|
gag
|
Mutation G330E in the v1 TRIM5alpha region exhibits a strong level of HIV-1 resistance, while mutations G330A or G330S have little or no effect |
PubMed
|
|
gag
|
The level of susceptibility hTRIM5alpha expressed by viruses carrying HIV-2 CA sequences in the context of HIV-1 NL4-3 is higher than that of HIV-1 NL4-3 and markedly higher than a panel of primary HIV-1 CA sequences |
PubMed
|
|
gag
|
HIV-1 CA-V86M mutant is partially resistant to restriction by hTRIM5alpha mutant R322G/R335G. The restriction of CA-V86M by hTRIM5alpha R322G/R335G is independent of cyclophilin A, but correlates with its sensitivity to cyclosporine A treatment |
PubMed
|
|
gag
|
TRIM5alpha allelic variants R136Q/H419Y and H43Y/G249D are generally inactive for HIV-1 CA inhibition |
PubMed
|
|
gag
|
The T216I mutation in HIV-1 CA restores the ability of P38A CA mutant particles to saturate TRIM5alpha host restrictions in monkey cells |
PubMed
|
|
gag
|
The TAK1 kinase complex (TAK1/TAB2/TAB3) contributes to capsid-specific restriction mediated by TRIM5alpha. TRIM5alpha activates TAK1 autophosphorylation |
PubMed
|
|
gag
|
Human TRIM5-alpha and TRIM5-delta proteins are dominant negative to HIV-1 restriction in rabbit cells |
PubMed
|
|
gag
|
TRIM5alpha associates with HIV-1 capsid-nucleocapsid complexes assembled in vitro, and the TRIM5alpha interaction with these complexes is dependent on its B30.2(SPRY) domains |
PubMed
|
|
gag
|
Cluster I-A and Cluster II-A changes in the B-box 2 domain of TRIM5alpha decrease its binding to HIV-1 Capsid |
PubMed
|
|
gag
|
Two B-box TRIM5alpha mutants (Cluster I-A:Q109E, E110K, V114A, I115L, and L118V; Cluster II-A:E120A, R121Q, Q123R, and E124K) abolish the weak restricting activity against HIV-1 associated with wild-type TRIM5alpha |
PubMed
|
|
gag
|
Human TRIM5alpha modestly, but specifically, inhibits an HIV-1 strain carrying a mutation (G89V) in the cyclophilin binding loop in capsid |
PubMed
|
|
gag
|
The effect of inhibition of CA-CypA interaction by TRIM5alpha is virus isolates-dependent, which can result in inhibition, no change, or an increase in viral infectivity |
PubMed
|
|
gag
|
TRIM5alpha binds to HIV-1 CA tubular assemblies in a dose-dependent manner, especially at P207/T216 inter-hexamer interfaces |
PubMed
|
|
nucleocapsid
|
gag
|
R332G/R335G and R330E/R332G/R335G mutants of TRIM5alpha binds the in vitro-assembled CA-NC complexes and the strength of the interaction correlates with the magnitude of restriction |
PubMed
|
|
gag
|
TRIM5alpha disrupts the regular cylindrical hexameric lattice structure of HIV-1 CA-NC complex |
PubMed
|