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Host cell protein kinases in nonsegmented negative-strand virus (mononegavirales) infection.

Abstract
Phosphorylation of one or more viral proteins is probably an essential step in the life cycle of every member of the nonsegmented negative-strand RNA virus (mononegavirales [MNV]) group. Since no virally encoded protein kinases have been discovered in this group, phosphorylation is effected entirely by host cell kinases. The virally encoded P proteins of the MNV are the only ones consistently phosphorylated with a stoichiometry > or =1. The P protein of vesicular stomatitis virus (VSV), and perhaps also of respiratory syncytial virus, are the only ones for which a function of phosphorylation has been established. Phosphorylation by casein kinase 2 at one or more identified sites in the VSV P protein activates transcriptional activity by promoting formation of a homotrimer, which is then capable of binding the RNA polymerase and attaching it to the N protein-RNA template. A second phosphorylation of VSV P protein by a different kinase also occurs, dependent upon prior modification by casein kinase 2, but its function is not definitely known. Phosphorylation of the other MNV P proteins may serve a different purpose. No evidence has been obtained yet for any function for phosphorylation of any other MNV protein.
AuthorsJ Lenard
JournalPharmacology & therapeutics (Pharmacol Ther) Vol. 83 Issue 1 Pg. 39-48 (Jul 1999) ISSN: 0163-7258 [Print] England
PMID10501594 (Publication Type: Journal Article, Review)
Chemical References
  • Protein Kinases
  • Casein Kinases
Topics
  • Casein Kinases
  • Humans
  • Mononegavirales (enzymology, metabolism)
  • Mononegavirales Infections (enzymology)
  • Phosphorylation
  • Protein Kinases (metabolism, physiology)
  • Transcription, Genetic
  • Vesicular stomatitis Indiana virus (enzymology, metabolism)

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