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Rev
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rev
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HIV-1 Rev disrupts both IN-TNPO3 and IN-importin alpha complexes |
PubMed
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rev
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The interaction of HIV-1 Rev with RAN or NUP98 hypothetically induces the binding of Rev to transportin 3 |
PubMed
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capsid
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gag
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TNPO3 is an export factor for both HIV-1 CA and tRNAs from the nucleus of infected cells |
PubMed
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gag
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HIV-1 inhibition by TNPO3 knockdown and CPSF6-358 is a CA-dependent manner and cytoplasmic localization of CPSF6-358 is required to inhibit HIV-1 |
PubMed
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gag
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TNPO3 directly interacts with in vitro-assembled HIV-1 CA-NC complexes. However, the other report that TNPO3 does not interact directly with HIV-1 CA tubes in vitro |
PubMed
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gag
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Cyclophilin A stabilizes the HIV-1 CA and antagonizes TNPO3 acceleration of uncoating in vitro |
PubMed
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gag
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HIV-1 N74D CA mutant remains partially dependent on TRN-SR2 for efficient infection when carrying the HIV envelope |
PubMed
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gag
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Residues N57, M66, Q67, K70, N74, and T107 in the N-terminal domain of HIV-1 CA are important for the binding to CPSF6. Mutations on these residues lead to the loss or reduction of dependency on TNPO3 and RanBP2 |
PubMed
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gag
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HIV-1 replication is dependent on TNPO3 expression and HIV-1 CA is the primary determinant for HIV-1 dependence upon TNPO3 |
PubMed
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gag
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Replacing HIV-1 CA with the corresponding MLV CA strikingly induce the chimera viruses insensitive to TNPO3 knockdown, suggesting that CA is a dominant viral determinant of TNPO3 dependency during HIV-1 infection |
PubMed
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gag
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HIV-1 CA and viral tRNAs bind to TNPO3 with greater affinity in the presence of RanGTP. The last 98 residues (amino acids 826-923) are important for CA and tRNA binding |
PubMed
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gag
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RanGTP inhibits the ability of TNPO3 to stimulate the uncoating of HIV-1 CA cores |
PubMed
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gag
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HIV-1 CA mutant with five amino acid substitutions (Q67H, K70R, H87P, T107N, and L111I) confers TNPO3-independence |
PubMed
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integrase
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gag-pol
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HIV-1 IN mutant R263A/K264A significantly reduces its ability of binding to TRN-SR2 and displays a block in nuclear import and integration |
PubMed
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gag-pol
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Site specific mutagenesis reveals that residues 185FKRK188 in the catalytic core domain (CCD) and 262RRK264 and K266/R269 in the C-terminal domain (CTD) in HIV-1 IN are important for its binding to TRN-SR2 |
PubMed
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gag-pol
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HIV-1 IN (amino acids 62-176) interacts with TRN-SR2 (amino acids 62-334) in yeast two-hybrid screen. TRN-SR2 imports the preintegration complex into the nucleus and TRN-SR2 knockdown inhibits early steps of HIV-1 replication |
PubMed
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gag-pol
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The binding between HIV-1 IN and TNPO3 is inhibited by RanGTP in a dose-dependent manner, leading to a TNPO3-RanGTP complex formation |
PubMed
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gag-pol
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R400E/R402E and Q761E/R762E substitutions in TNPO3 significantly impair its binding to HIV-1 IN. However, E304R and E391R/E392R have very little effect on the IN-TNPO3 interaction |
PubMed
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gag-pol
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Peptides (amino acids 170-191, 214-229, and 262-274) derived the C-terminal domain of HIV-1 IN bind to TRN-SR2 |
PubMed
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gag-pol
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HIV-1 Rev disrupts both IN-TNPO3 and IN-importin alpha complexes |
PubMed
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nucleocapsid
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gag
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TNPO3 directly interacts with in vitro-assembled HIV-1 CA-NC complexes |
PubMed
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