vpx Antibody

1. These results indicate that Vpx, in addition to SAMHD1, overcomes a previously unappreciated restriction for lentiviruses at the level of reverse transcription (RT)that acts independently of dNTP concentrations and is specific to resting CD4 T cells. PMID: 28228523
2. zinc binding appears to mitigate flexibility of the three-helix fold of Vpx, thereby preventing dysfunction. PMID: 28284276
3. Data indicate that proline residue P109 within the C-terminal poly-proline motif (PPM) of Vpx protein plays a unique role in the regulation of SAM domain and HD domain 1 protein SAMHD1 degradation. PMID: 25936766
4. HIV-2 Vpr can trigger G2 cell cycle arrest through either CUL4A or CUL4B. PMID: 24719410
5. Vpx expression results in decreased promoter binding activity of IRF5 PMID: 24532789
6. Poly-proline motif in Vpx is critical for its efficient expression in cells. PMID: 24114794
7. Data suggest that, in an evolutionary model of virus-host interactions, binding of Vpx/Vpr with SAMHD1 (and subsequent degradation of SAMHD1 [SAM domain/HD domain-containing protein 1]) exhibits dynamic requirements that have toggled back and forth. PMID: 23874202
8. the crystal structure of a ternary complex of Vpx with the human E3 ligase substrate adaptor DCAF1 and the carboxy-terminal region of human SAMHD1 PMID: 24336198
9. direct down-modulation of Vpx catalytic activity, mediated by the same binding event that leads to SAMHD1 recruitment to the E3 ubiquitin ligase for proteasome-dependent degradation PMID: 23677995
10. Effective immune control of viral replication in HIV-2-infected individuals is not associated with increased Vpx-mediated degradation of SAMHD1. PMID: 23497283
11. there are several Vpx residues required for SAMHD1 degradation PMID: 23076149
12. The Vpx lentiviral accessory protein targets human SAMHD1 for degradation in the nucleus. PMID: 22973040
13. Vpx targets SAMHD1 for degradation in a viral strategy to control cellular deoxynucleotide levels for efficient replication PMID: 22069334
14. structure and cytopathogenic activity PMID: 16153874
15. These studies map critical residues of the Vpx nuclear localization signal that are required for efficient infection of non-dividing cells. PMID: 16325220
16. We found that insertion within the polyproline-containing C-terminus destabilizes nuclear localization, whereas mutating a second helix in the central domain disrupts viral packaging. PMID: 16457868
17. results indicated that Vpx and Vpr of HIV-2 may cooperatively contribute to virion infectivity without affecting virion morphogenesis PMID: 16953064
18. The results here clearly demonstrated that the entire Vpx protein is critical for reverse transcription of the HIV-2 genome in human monocyte-derived macrophages. PMID: 18495778
19. when transferred in the context of a replication-competent viral clone, Vpx was required for replication in dendritic cells PMID: 18829761
20. Vpx diverts the Cul4A-DDB1(DCAF1) ligase to inactivate an evolutionarily conserved factor, which restricts macrophage infection by HIV-2. PMID: 19264781

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KEGG: vg:1724714