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.

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147 ganisms and without cross-resistance to the majority of other clinically useful an ti biotics. Oleandomycin is an agent which, with the exception of cross-resistance to members of the erythromycin group, displays these properties.Summary (1) In vitro under the specific conditions of the gradient plate technic, combinations of sulfisoxazole and oleandomycin in specific ratios show an activity superior to that observed with the single constituents.( 2 ) Supplemental activity was also observed in vivo in the streptococcal, staphylococcal and pneumococcal infections when the ratio of the combination of sulfisoxazole to oleandomycin was 5 to 1. ( 3 ) The same type of effect was also observed in Salmonella schottmuelleri infection of mice when activity of sulfisoxazole was determined in a constant, inactive amount of oleandomycin.The authors wish to express their gratitude to Miss A. Bagnole, Miss J. Giamportone and Miss J. Tinsley who cooperated in carrying out the experiments.

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