Solubilization of a protein synthesis inhibitor from vaccinia virions

Author:

Ben-Hamida F,Person A,Beaud G

Abstract

The protein synthesis inhibitor previously demonstrated to be associated with vaccinia cores was quantitatively solubilized from vaccinia virions or cores after an endogenous protein kinase reaction at pH 10. The presence of the inhibitor in the soluble extract correlated with the presence of soluble virion proteins phosphorylated in vitro. Partially purified inhibitor blocked methionyl-tRNAfMet-40S initiation complex formation, as was the case in cell-free extracts derived from vaccinia virus-infected cells.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference16 articles.

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2. Studies on the mechanisms of vaccinia virus cytopathic effects. I. Inhibition of protein synthesis in infected cells is associated with virus-induced RNA synthesis;Bablanan R.;J. Gen. Virol.,1978

3. In vitro inhibition of protein synthesis by purified cores from vaccinia virus;Ben-Hamida F.;Proc. Nati. Acad. Sci. U.S.A.,1978

4. Endogenous protein kinase and phosphate acceptor protein in vaccinia virus;Downer D. N.;Virology,1973

5. Early virus protein synthesis in vaccinia virus-infected cells;Esteban M.;J. Gen. Virol.,1973

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