Phosphorylation of rabies virus proteins was followed and . The N and M proteins were both found to be phosphorylated. The M protein was present in the virion in two phosphorylated states, but only the hypophosphorylated form of M was found in infected cells. The hypothesis that some of the M molecules become hyperphosphorylated during the maturation process by a membrane-bound kinase was examined. The phosphorylation of the viral proteins by the kinase present in purified rabies virions was studied using an transcriptase assay: under the conditions of the assay, additional phosphate groups were rapidly attached to the N protein. The M protein was similarly hyperphosphorylated although more slowly. Whether the hyperphosphorylation of the N protein is responsible for the poor efficiency of the transcriptase reaction is not clear. No detectable change in the phosphorylation of cellular proteins was observed in the course of rabies virus infection.


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