This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Serhir, B. Articles by Jacques, M. Search for Related Content PubMed PubMed Citation Articles by Serhir, B. Articles by Jacques, M.

 Previous Article  |  Next Article 

J. Bacteriol., Jul 1995, 3830-3836, Vol 177, No. 13
Copyright © 1995, American Society for Microbiology

Purification and characterization of a 52-kilodalton immunoglobulin G- binding protein from Streptococcus suis capsular type 2

B Serhir, D Dubreuil, R Higgins and M Jacques
Departement de Pathologie et Microbiologie, Faculte de Medecine Veterinaire, Universite de Montreal, St-Hyacinthe, Quebec, Canada.

We previously reported that group D streptococci exhibited immunoglobulin G (IgG)-binding activity and that a 52-kDa IgG-binding protein was present in all Streptococcus suis strains examined (B. Serhir, R. Higgins, B. Foiry, and M. Jacques, J. Gen. Microbiol. 139:2953-2958, 1993). The objective of the present study was to purify and characterize this protein. Pig IgG were immobilized through their Fab fragments to ECH-Sepharose 4B, and the protein was purified by affinity chromatography. Electron microscopy observations of the purified material showed filamentous structures with a diameter of approximately 4 nm; these structures were not observed when the material was treated with either urea or ethanolamine. Electrophoretic and Western immunoblot analyses showed that the 52-kDa protein constituted the bulk of the recovered material. This protein was stained with either Coomassie brilliant blue or silver nitrate; it reacted with a large variety of mammalian IgG, human IgG (Fc) fragments, human IgA, and other human plasma proteins. The 52-kDa protein exhibited lower IgG-binding affinities than protein A and protein G. However, it was able to compete with protein A and protein G for binding to human IgG. In addition, it bound chicken IgG with high affinity. This last property differentiated the 52-kDa protein of S. suis from the six IgG-binding proteins described to date. The 52-kDa protein displayed similar affinities for untreated and deglycosylated pig IgG. The N-terminal amino acid sequence (SIITDVYAXEVLDSXGNPTLEV) revealed no homology with any bacterial proteins in the Swiss-Prot database.(ABSTRACT TRUNCATED AT 250 WORDS)

This article has been cited by other articles:

• Li, Y., Martinez, G., Gottschalk, M., Lacouture, S., Willson, P., Dubreuil, J. D., Jacques, M., Harel, J. (2006). Identification of a Surface Protein of Streptococcus suis and Evaluation of Its Immunogenic and Protective Capacity in Pigs. Infect. Immun. 74: 305-312 [Abstract] [Full Text]  
• Jobin, M.-C., Brassard, J., Quessy, S., Gottschalk, M., Grenier, D. (2004). Acquisition of Host Plasmin Activity by the Swine Pathogen Streptococcus suis Serotype 2. Infect. Immun. 72: 606-610 [Abstract] [Full Text]  
• Song, X.-M., Perez-Casal, J., Fontaine, M. C., Potter, A. A. (2002). Bovine immunoglobulin A (IgA)-binding activities of the surface-expressed Mig protein of Streptococcus dysgalactiae. Microbiology 148: 2055-2064 [Abstract] [Full Text]