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 VP, VP and VP of the virus. Immunoprecipitations with antisera against whole virus and VP indicated the synthesis of VP and of at least two additional peptides of 100000 and 56000 daltons containing antigenic sites of VP. 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 NCVP. The amount of foot-and-mouth disease virus and VP-specific peptides in the virus RNA-directed products were measured by immunoprecipitation.


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