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

 Previous Article  |  Next Article 

Infection and Immunity, February 2002, p. 803-811, Vol. 70, No. 2
0019-9567/01/$04.00+0     DOI: 70.2.803-811.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Molecular Analysis of Group B Protective Surface Protein, a New Cell Surface Protective Antigen of Group B Streptococci

Sezgin Erdogan,1 Peter K. Fagan,1 Susanne R. Talay,1 Manfred Rohde,1 Patricia Ferrieri,2 Aurea E. Flores,2 Carlos A. Guzmán,1 Mark J. Walker,3 and Gursharan S. Chhatwal1*

Department of Microbial Pathogenesis and Vaccine Research, GBF--German Research Centre for Biotechnology, 38124 Braunschweig, Germany,1 Departments of Laboratory MedicinePathology and Pediatrics, University of Minnesota Medical School and Hospital, University of Minnesota, Minneapolis, Minnesota,2 Department of Biological Sciences, University of Wollongong, Wollongong, NSW 2522, Australia3

Received 23 August 2001/ Returned for modification 30 October 2001/ Accepted 12 November 2001

Group B streptococci (GBS) express various surface antigens designated c, R, and X antigens. A new R-like surface protein from Streptococcus agalactiae strain Compton R has been identified by using a polyclonal antiserum raised against the R protein fraction of this strain to screen a lambda Zap library. DNA sequence analysis of positive clones allowed the prediction of the primary structure of a 105-kDa protein designated BPS protein (group B protective surface protein) that exhibited typical features of streptococcal surface proteins such as a signal sequence and a membrane anchor region but did not show significant similarity with other known sequences. Immunogold electron microscopy using a BPS-specific antiserum confirmed the surface location of BPS protein on S. agalactiae strain Compton R. Anti-BPS antibodies did not cross-react with R1 and R4 proteins expressed by two variant type III GBS strains but reacted with the parental streptococcal strain in Western blot and immunoprecipitation analyses. Separate R3 and BPS immunoprecipitation bands were observed when a cell extract of strain Compton R was tested with an antiserum against Compton R previously cross-absorbed to remove R4 antibodies. Immunization of mice with recombinant BPS protein by the subcutaneous route produced an efficient antigen-specific response, and immunized animals survived challenge with a lethal dose of a virulent strain. Therefore, BPS protein represents a new R-like protective antigen of GBS.

* Corresponding author. Mailing address: GBF--German Research Centre for Biotechnology, Mascheroder Weg 1, 38124 Braunschweig, Germany. Phone: 49 531 6181-297. Fax: 49 531 6181-708. E-mail: gsc{at}gbf.de.

Editor: D. L. Burns

Infection and Immunity, February 2002, p. 803-811, Vol. 70, No. 2
0019-9567/01/$04.00+0     DOI: 70.2.803-811.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Nobbs, A. H., Lamont, R. J., Jenkinson, H. F. (2009). Streptococcus Adherence and Colonization. Microbiol. Mol. Biol. Rev. 73: 407-450 [Abstract] [Full Text]  
  • Mavenyengwa, R. T., Maeland, J. A., Moyo, S. R. (2009). Putative Novel Surface-Exposed Streptococcus agalactiae Protein Frequently Expressed by the Group B Streptococcus from Zimbabwe. CVI 16: 1302-1308 [Abstract] [Full Text]  
  • Mavenyengwa, R. T., Maeland, J. A., Moyo, S. R. (2008). Distinctive Features of Surface-Anchored Proteins of Streptococcus agalactiae Strains from Zimbabwe Revealed by PCR and Dot Blotting. CVI 15: 1420-1424 [Abstract] [Full Text]  
  • Ramaswamy, S. V., Ferrieri, P., Flores, A. E., Paoletti, L. C. (2006). Molecular characterization of nontypeable group B streptococcus.. J. Clin. Microbiol. 44: 2398-2403 [Abstract] [Full Text]  
  • Maeland, J. A., Bevanger, L., Lyng, R. V. (2005). Immunological Markers of the R4 Protein of Streptococcus agalactiae. CVI 12: 1305-1310 [Abstract] [Full Text]  
  • Lindahl, G., Stalhammar-Carlemalm, M., Areschoug, T. (2005). Surface Proteins of Streptococcus agalactiae and Related Proteins in Other Bacterial Pathogens. Clin. Microbiol. Rev. 18: 102-127 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»