Role of the LXX repeats of the HIV-1 and SIV sm Gag p6 domain in Vpr
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Download scientific diagram | Role of the LXX repeats of the HIV-1 and SIV sm Gag p6 domain in Vpr and Vpx binding. (A) Mutation within the p6 (LXX) 4 region disrupts HIV-1 Vpr binding to Pr55 Gag. A diagram shows the HIV-1 wt Pr55 Gag and GagL44A mutant. The p6 (LXX) 4 repeats are underlined, and the Leu residue replaced by Ala in the GagL44A mutant is indicated by an asterisk. Numbering refers to the HIV-1 Lai p6 domain (30). L40 expressing HIV-1 Vpr fused to the LexABD and either Gagp6 (lane 1), GagL44A (lane 2), or Pr55 Gag wt (lane 3) fused to the Gal4AD was analyzed for-gal activity. The filter assay was carried out overnight. (B) Quantitative-gal assay of SIV sm Vpr and Vpx binding to Gag and p6 mutants. A diagram shows the SIV sm Gag wt and GagL54A, GagL1, GagL2, and GagL3 mutants. The p6 (LXX) 3 repeats are underlined, and the Leu residue replaced by Ala in the GagL54A mutant is indicated by an asterisk. Numbering refers to the SIVsmPbj1.9 p6 domain (30). L40 expressing either the SIV sm Vpr (solid bars) or Vpx (white bars) LexABD hybrid in combination with each of the Gal4AD hybrids indicated was assayed for-gal activity in a liquid culture assay. The results are expressed as the percentages of the-gal activity determined for each Gag or p6 mutant relative to the activity obtained with the wt Gag and p6, respectively. The background level is approximately 2 U and corresponds to L40 expressing either the SIV sm Vpr-or Vpx-LexABD hybrid and the Gal4AD-Raf hybrid. from publication: Interaction with the p6 Domain of the Gag Precursor Mediates Incorporation into Virions of Vpr and Vpx Proteins from Primate Lentiviruses | Vpr and Vpx proteins from human and simian immunodeficiency viruses (HIV and SIV) are incorporated into virions in quantities equivalent to those of the viral Gag proteins. We demonstrate here that Vpr and Vpx proteins from distinct lineages of primate lentiviruses were able | Virion, Simian Immunodeficiency Virus and HIV | ResearchGate, the professional network for scientists.
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