The vesicular stomatitis virus L protein possesses the mRNA methyltransferase activities

Virology. 1988 Mar;163(1):222-5. doi: 10.1016/0042-6822(88)90253-x.


We have previously shown that the vesicular stomatitis virus (VSV) host range mutant, hr 1, is completely defective for the mRNA methyltransferase activities, but can synthesize full-length, unmethylated mRNAs in vitro [S. M. Horikami and S. A. Moyer (1982). Proc. Natl. Acad. Sci. USA 79, 7694-7698] and in vivo [S. M. Horikami, F. De Ferra, and S. A. Moyer (1984). Virology 138, 1-15]. Here we have used the hr 1 mutant to identify the viral protein which possesses the methyltransferase activities. The wild-type VSV L and NS proteins, subunits of the viral RNA polymerase, were separately purified and added to high salt dissociated mutant hr 1 nucleocapsids for in vitro transcription reactions. The results show that the purified wild-type L protein, but not the NS protein, restores methylation and thus possesses the viral mRNA methyltransferase activities.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Capsid / isolation & purification
  • Capsid / metabolism
  • Methylation
  • Methyltransferases / metabolism*
  • Mutation
  • RNA Replicase / metabolism
  • RNA, Messenger / biosynthesis
  • RNA, Messenger / metabolism
  • RNA, Viral / biosynthesis
  • RNA, Viral / metabolism
  • Transcription, Genetic
  • Vesicular stomatitis Indiana virus / enzymology*
  • Vesicular stomatitis Indiana virus / genetics
  • Viral Core Proteins / isolation & purification
  • Viral Core Proteins / metabolism
  • Viral Nonstructural Proteins
  • Viral Proteins / isolation & purification
  • Viral Proteins / metabolism*


  • RNA, Messenger
  • RNA, Viral
  • Viral Core Proteins
  • Viral Nonstructural Proteins
  • Viral Proteins
  • Methyltransferases
  • L protein, vesicular stomatitis virus
  • RNA Replicase