The herpes simplex virus vhs protein induces accelerated RNA decay through endoribonucleolytic cleavage, requiring Mg(2+) and occurring independently of ribosomes.
The HSV vhs protein induces RNA decay via endoribonucleolytic cleavage independent of ribosomes, 5' caps, or 3' poly(A) tails.
The herpes simplex virus virion host shutoff (vhs) protein (UL41 gene product) is a component of the HSV virion tegument that triggers shutoff of host protein synthesis and accelerated mRNA degradation during the early stages of HSV infection. Previous studies have demonstrated that extracts from HSV-infected cells and partially purified HSV virions display vhs-dependent RNase activity and that vhs is sufficient to trigger accelerated RNA degradation when expressed as the only HSV protein in an in vitro translation system derived from rabbit reticulocytes. We have used the rabbit reticulocyte translation system to characterize the mode of vhs-induced RNA decay in more detail. We report here that vhs-dependent RNA decay proceeds through endoribonucleolytic cleavage, is not affected by the presence of a 5' cap or a 3' poly(A) tail in the RNA substrate, requires Mg(2+), and occurs in the absence of ribosomes. Intriguingly, sites of preferential initial cleavage were clustered over the 5' quadrant of one RNA substrate that was characterized in detail. The vhs homologue of pseudorabies virus also induced accelerated RNA decay in this in vitro system.
Elgadi et al. (Wed,) conducted a other in Herpes simplex virus infection. Herpes simplex virus vhs protein was evaluated on RNA decay mechanism. The herpes simplex virus vhs protein induces accelerated RNA decay through endoribonucleolytic cleavage, requiring Mg(2+) and occurring independently of ribosomes.