A DNA sequence coding for the immunogenic capsid protein VP3 of foot-and-mouth disease virus A12, prepared from the virion RNA, was ligated to a plasmid designed to express a chimeric protein from the Escherichia coli tryptophan promoter-operator system. When Escherichia coli transformed with this plasmid was grown in tryptophan-depleted media, approximately 17 percent of the total cellular protein was found to be an insoluble and stable chimeric protein. The purified chimeric protein competed equally on a molar basis with VP3 for specific antibodies to foot-and-mouth disease virus. When inoculated into six cattle and two swine, this protein elicited high levels of neutralizing antibody and protection against challenge with foot-and-mouth disease virus.

Partly cooked canned hams and dried pepperoni and salami sausages were prepared from the carcasses of pigs infected with African swine fever virus and pigs infected with hog cholera virus. Virus was not recovered from the partly cooked canned hams; however, virus was recovered in the hams before heating in both instances. Both African swine fever virus and hog cholera virus were recovered from the dried salami and pepperoni sausages, but not after the required curing period.

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