Identification of a new region in the vesicular stomatitis virus L polymerase protein which is essential for mRNA cap methylation

Virology
Valery Z GrdzelishviliS A Moyer

Abstract

The vesicular stomatitis virus (VSV) L polymerase protein possesses two methyltransferase (MTase) activities, which catalyze the methylation of viral mRNA cap structures at the guanine-N7 and 2'-O-adenosine positions. To identify L sequences required for the MTase activities, we analyzed a host range (hr) and temperature-sensitive (ts) mutant of VSV, hr8, which was defective in mRNA cap methylation. Sequencing hr8 identified five amino acid substitutions, all residing in the L protein. Recombinant VSV were generated with each of the identified L mutations, and the presence of a single G1481R substitution in L, located between conserved domains V and VI, was sufficient to produce a dramatic reduction (about 90%) in overall mRNA methylation. Cap analysis showed residual guanine-N7 methylation and reduced 2'-O-adenosine methylation, identical to that of the original hr8 virus. When recombinant viruses were tested for virus growth under conditions that were permissive and nonpermissive for the hr8 mutant, the same single L mutation, G1481R, was solely responsible for both the hr and ts phenotypes. A spontaneous suppressor mutant of the rG1481R virus that restored both growth on nonpermissive cells and cap methylation was identified...Continue Reading

References

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Dec 3, 2004·The Journal of Biological Chemistry·Tomoaki OginoKiyohisa Mizumoto

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Citations

Dec 5, 2008·Journal of Virology·Andrea M Murphy, Valery Z Grdzelishvili
Oct 14, 2009·Virology Journal·Megan Moerdyk-SchauweckerValery Z Grdzelishvili
Aug 25, 2009·Archives of Virology·Nobuyuki MochizukiTakeo Sakai
Jul 9, 2010·Virology·Andrea M MurphyValery Z Grdzelishvili
Jun 26, 2013·Virus Research·Eric HastieValery Z Grdzelishvili
May 22, 2021·Antiviral Research·Joyce Sweeney GibbonsChristopher F Basler

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