Phosphorylation of Vesicular Stomatitis Virus In Vivo and In Vitro

摘要: The structural protein, NS, of purified vesicular stomatitis virus (VSV) is a phosphoprotein. In infected cells phosphorylated NS found both free in the cytoplasm and as part viral ribonucleoprotein (RNP) complex containing 42S RNA proteins L, N, indicating that phosphorylation occurs an early event maturation. VSV contains endogenous protein kinase activity, probably host region, which catalyzes vitro M, but not N or G. sites on appear to be different vivo reactions, are differentially sensitive alkaline phosphatase. After removal membrane components with dextran-polyethylene glycol two-phase separation, activity remains tightly associated RNP. However, RNP isolated from shows only small amount activity. enzyme appears cellular contaminant because uninfected cell extract can phosphorylate dissociated M. virion-associated may derived either plasma since these contain similar VSV.