PRODUCTION AND IDENTIFICATION OF RECOMBINANT PROTEINS OF SALMONELLA-TYPHIMURIUM AND THEIR USE IN DETECTION OF ANTIBODIES IN EXPERIMENTALLY CHALLENGED ANIMALS

Antibodies to experimental Salmonella typhimurium challenge in cattle and sheep were assessed by 15 recombinant flagellum proteins. The 15 D NA fragments selected for gene expression were derived from external f lagellin, hook, hook-associated protein, and basal body gene domains. Our efforts were focused on characterizing the humoral immune response of Salmonella infected and vaccinated animals and identifying immunod ominant antigenic determinants. This communication reports that the 15 9-261 amino acids of external flagellum (FliCi-1), 285-331 amino acids of hook protein (FlgE-2), and 309-391 amino acids and 440-537 amino a cids of hook-associated protein (FLgK-1 and -2) appeared to be the mos t immunoreactive proteins and were recognized by all of the experiment al animal sera tested in this study.