Abstract
A particulate fraction of Erysipelothrix rhusiopathiae cultures has been subjected to butanol extraction and treatment with surface-active agents in an attempt to solubilize a protective antigen. The particulate fraction was partitioned into the butanol layer but was not solubilized. Only sodium dodecyl sulfate solubilized the particles. The soluble protective activity was not sedimented by centrifugation at 198,000 x g for 12 hr but was excluded by Sephadex G-200. Immunodiffusion studies of the soluble fraction demonstrated eight antigens, five of horse serum origin and three of E. rhusiopathiae origin. Ultracentrifugation indicated that spontaneous reaggregation occurred after removal of the sodium dodecyl sulfate. Analytical ultracentrifugation showed that 90% of the sodium dodecyl sulfatetreated material migrated as a single homogeneous 3.5S component. The physical and biological characteristics of the protective activity suggest that the protective antigen is a glyco-lipoprotein.
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