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.