Host-dependent phosphorylation and kinase activity associated with vesicular stomatitis virus

Abstract

Among the protein kinases associated with vesicular stomatitis virus (VSV), one was identified by immunoprecipitation to be pp60src, the transformation-specific product coded for by avian sarcoma virus, or its endogenous cellular homolog. This activity phosphorylated only tyrosine. pp60src was enriched in the membranes, whereas the serine- and threonine-specific kinases were concentrated with viral cores. The content of pp60src in VSV can be manipulated by growing VSV in different host cells. Monolayer baby hamster kidney cells transformed by an avian sarcoma virus produced VSV progeny which contained 7-fold greater pp60src activity than progeny produced by control untransformed or revertant cells. In contrast, suspension cultures of baby hamster kidney cells which produced VSV with increased tyrosine-specific kinase activity did not affect the content of pp60src. When pp60src was specifically increased in cells, the endogenous phosphorylation of tyrosine residues in the VSV matrix M protein was also enhanced, to as much as 20-fold. The phosphorylation of serine or threonine in this protein or in the other VSV phosphoprotein NS was not affected. Cellular tyrosine-specific kinases other than pp60scr did not change the overall phosphorylation pattern of any VSV phosphoproteins. Experiments designed to test the effects of endogenous phosphorylation on the various functions of the M protein failed to detect any significant alterations.