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Cell-Free Translation of Foot-and-Mouth Disease Virus RNA into Identifiable Non-capsid and Capsid Proteins

H. L. Bachrach

Plum Island Animal Disease Center, Agricultural Research Service, U.S. Department of Agriculture, Greenport, New York 11944, U.S.A.

Foot-and-mouth disease virus (a member of the picornavirus group) RNA could be translated effectively in an S-30 extract from Ehrlich ascites tumour cells. This translation was inhibited by aurintricarboxylic acid, cycloheximide, puromycin and RNase. Cell-free products of translation were identified by disc gel electrophoresis and immunoprecipitation with specific antisera. Gel electrophoresis of the products without prior immunoprecipitation suggested the synthesis of some of the non-capsid proteins and capsid proteins VP₁, VP₂ and VP₃ of the virus. Immunoprecipitations with antisera against whole virus and VP₃ indicated the synthesis of VP₃ and of at least two additional peptides of 100000 and 56000 daltons containing antigenic sites of VP₃. Gel electrophoresis after immunoprecipitation with antiserum against virus infection-associated antigen indicated the synthesis of a different 56000-dalton protein appearing to resemble non-capsid protein NCVP₅. The amount of foot-and-mouth disease virus and VP₃-specific peptides in the virus RNA-directed products were measured by immunoprecipitation.

^* Present address: Division of Laboratories and Research, Infectious Disease Laboratory, N.Y. State Department of Health, New Scotland Avenue, Albany, New York 12201.

To whom reprint requests should be sent.

Received 30 December 1975; accepted 14 April 1976.

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