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Journal of Virology, September 1999, p. 7153-7164, Vol. 73, No. 9
Departments of
Biology1 and
Pathology,2 McMaster University,
Hamilton, Ontario, Canada L8N 3Z5, and Department of Medical
Microbiology & Immunology, University of Alberta, Edmonton, Alberta,
Canada T6G 2H73
Received 19 March 1999/Accepted 24 May 1999
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
Mg2+, 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.
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
The Herpes Simplex Virus vhs Protein Induces
Endoribonucleolytic Cleavage of Target RNAs in Cell Extracts
*
Corresponding author. Mailing address: Department of
Medical Microbiology & Immunology, 1-41, Medical Sciences Bldg.,
University of Alberta, Edmonton, Alberta, Canada T6G 2H7. Phone: (780)
492-2308. Fax: (780) 492-7521. E-mail:
jim.smiley{at}ualberta.ca.
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