Figures
Induction of G2/M cell cycle arrest by the HIV-1 viral protein R (Vpr) requires the formation of mobile chromatin-associated foci.
Confocal immunofluorescence analysis of HeLa cells expressing the HIV-1 Vpr accessory protein. The picture shows the accumulation of Vpr (red) into discrete foci dispersed in the nucleus (the nuclear membrane is delineated by an anti-nucleoporin staining shown in blue). These foci contain the E3 ubiquitin ligase component VprBP (Vpr-binding protein, DCAF1), associate with chromatin, and display rapid saltatory movement inside the nucleus. Interference with the formation or function of these subnuclear structures through genetic manipulations or other means inevitably impairs the induction of G2/M arrest by Vpr, demonstrating their critical contributions to the cytostatic properties of the viral protein (see Belzile et al., doi:10.1371/journal.ppat.1001080).
Image Credit: Levon G. Abrahamyan, Institut de Recherches Cliniques de Montréal (IRCM)
Citation: (2010) PLoS Pathogens Issue Image | Vol. 6(9) September 2010. PLoS Pathog 6(9): ev06.i09. https://doi.org/10.1371/image.ppat.v06.i09
Published: September 30, 2010
Copyright: © 2010 Levon G. Abrahamyan. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Confocal immunofluorescence analysis of HeLa cells expressing the HIV-1 Vpr accessory protein. The picture shows the accumulation of Vpr (red) into discrete foci dispersed in the nucleus (the nuclear membrane is delineated by an anti-nucleoporin staining shown in blue). These foci contain the E3 ubiquitin ligase component VprBP (Vpr-binding protein, DCAF1), associate with chromatin, and display rapid saltatory movement inside the nucleus. Interference with the formation or function of these subnuclear structures through genetic manipulations or other means inevitably impairs the induction of G2/M arrest by Vpr, demonstrating their critical contributions to the cytostatic properties of the viral protein (see Belzile et al., doi:10.1371/journal.ppat.1001080).
Image Credit: Levon G. Abrahamyan, Institut de Recherches Cliniques de Montréal (IRCM)