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Characterization of a protective protein antigen of Erysipelothrix rhusiopathiae

Published online by Cambridge University Press:  15 May 2009

M. H. Groschup
Affiliation:
Department of Microbiology, Immunology and Parasitology, NYSCVM, Cornell University, Ithaca,NY 14850, USA
K. Cussler
Affiliation:
Paul-Ehrlich-Institut, Federal Agency for Sera and Vaccines, Paul-Ehrlich-Str. 51–59, 6070 Langen, Federal Republic of Germany
R. Weiss
Affiliation:
Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität, Frankfurter Str. 89, 6300 Giessen, Federal Republic of Germany
J. F. Timoney
Affiliation:
Department of Microbiology, Immunology and Parasitology, NYSCVM, Cornell University, Ithaca,NY 14850, USA
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Although vaccination is widely practiced against infection by Erysipelothrix rhusiopathiae in pigs and turkeys, the protective antigen(s) involved have not been fully characterized or purified to homogeneity. Antigens of E. rhusiopathiae strain T28, serotype 2b, and of FRANKFURT XI, serotype N, in culture supernatant and in extracts made with hot acid, 10 mM NaOH, ultrasound or EDTA were compared by SDS-PAGE and immunoblotting and in a mouse protection test. EDTA and 10 mM NaOH yielded highly protective extracts; culture supernatant was less protective and ultrasonic or hot acid extracts stimulated little or no protection in mice. Protective antisera from swine, horses and mice recognized prominent bands of molecular mass (m.m.) of 66–64 and 40–39 kDa in EDTA and 10 mM NaOH extracts. Mice immunized with preparations of the 66–64 kDa band purified by preparative electrophoresis were protected. Both antigens were trypsin sensitive, contained no detectable polysaccharide, and showed a marked tendency to aggregate in the absence of SDS.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1991

References

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