HIV-1 Vpr oligomerization but not that of Gag directs the interaction between Vpr and Gag.

Journal of Virology
Joëlle V FritzH de Rocquigny

Abstract

During HIV-1 assembly, the viral protein R (Vpr) is incorporated into newly made viral particles via an interaction with the C-terminal domain of the Gag polyprotein precursor Pr55(Gag). Vpr has been implicated in the nuclear import of newly made viral DNA and subsequently in its transcription. In addition, Vpr can affect the cell physiology by causing G(2)/M cell cycle arrest and apoptosis. Vpr can form oligomers, but their roles have not yet been investigated. We have developed fluorescence lifetime imaging microscopy-fluorescence resonance energy transfer-based assays to monitor the interaction between Pr55(Gag) and Vpr in HeLa cells. To that end, we used enhanced green fluorescent protein-Vpr that can be incorporated into the virus and tetracysteine (TC)-tagged Pr55(Gag)-TC. This TC motif is tethered to the C terminus of Pr55(Gag) and does not interfere with Pr55(Gag) trafficking and the assembly of virus-like particles (VLPs). Results show that the Pr55(Gag)-Vpr complexes accumulated mainly at the plasma membrane. In addition, results with Pr55(Gag)-TC mutants confirm that the (41)LXXLF domain of Gag-p6 is essential for Pr55(Gag)-Vpr interaction. We also report that Vpr oligomerization is crucial for Pr55(Gag) recognition ...Continue Reading

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Citations

Jun 28, 2011·Biochimie·Vanille J GreinerHugues de Rocquigny
Apr 20, 2014·Frontiers in Microbiology·Carolin A GuenzelSerge Benichou
Jul 1, 2016·Microbiology and Molecular Biology Reviews : MMBR·Guangdi Li, Erik De Clercq
Dec 4, 2019·Methods and Applications in Fluorescence·Julien Godet, Yves Mely
Oct 28, 2019·Cells·Helena Fabryova, Klaus Strebel
Sep 24, 2011·Methods : a Companion to Methods in Enzymology·Michael A Whitt, Chad E Mire

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