Nuclear herpesvirus capsid motility is not dependent on F-actin.
Bottom Line: However, the conclusions from these studies were indirect.Moreover, in these cells, three F-actin-inhibiting drugs failed to effect capsid motility.We revisited this phenomenon and found no evidence that nuclear capsid motility depended on F-actin.
Affiliation: Department of Molecular Biology, Princeton University, Princeton, New Jersey, USA Princeton Neuroscience Institute, Princeton University, Princeton, New Jersey, USA.Show MeSH
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Mentions: As the previous result suggested a direct binding of nuclear capsids to actin rods, we next sought to show this interaction biochemically. To this end, we infected MEF-LA with capsid-tagged PRV and treated with LatA as described above. We then lysed the cells and used an anti-GFP antibody to immunoprecipitate Lifeact-GFP and associated proteins. By Western blotting, we detected Lifeact-GFP and actin in the immunoprecipitates of all conditions. However, only in the LatA-treated cells did we detect the major capsid protein VP5 (Fig. 5). Thus, we conclude that LatA-induced actin rods most likely trap intranuclear capsids by binding them, leading to the observed drop in motility by live-cell microscopy. This provides an intriguing alternative explanation of how LatA leads to intranuclear capsid stalling and provides a good model for why LatA influences capsid motility but the other tested F-actin-depolymerizing drugs do not.
Affiliation: Department of Molecular Biology, Princeton University, Princeton, New Jersey, USA Princeton Neuroscience Institute, Princeton University, Princeton, New Jersey, USA.