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 Siboo, I. R.
Right arrow Articles by Sullam, P. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Siboo, I. R.
Right arrow Articles by Sullam, P. M.

 Previous Article  |  Next Article 

Infection and Immunity, April 2005, p. 2273-2280, Vol. 73, No. 4
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.4.2273-2280.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Role of SraP, a Serine-Rich Surface Protein of Staphylococcus aureus, in Binding to Human Platelets

Ian R. Siboo,1,2 Henry F. Chambers,2,3 and Paul M. Sullam1,2*

Division of Infectious Diseases, Veterans Affairs Medical Center,1 Division of Infectious Diseases, San Francisco General Hospital,3 Department of Medicine, University of California, San Francisco, California2

Received 10 August 2004/ Returned for modification 1 October 2004/ Accepted 14 December 2004

The binding of bacteria to platelets is a postulated central event in the pathogenesis of infective endocarditis. Platelet binding by Streptococcus gordonii is mediated in large part by GspB, a high-molecular-mass cell wall glycoprotein. Although Staphylococcus aureus has a GspB homolog (SraP), little is known about its function. SraP has a calculated molecular mass of 227 kDa and, like GspB, is predicted to contain an atypical N-terminal signal sequence, two serine-rich repeat regions (srr1 and srr2) separated by a nonrepeat region, and a C-terminal cell wall anchoring motif (LPDTG). To assess whether SraP contributes to platelet binding, we compared the binding to human platelets of S. aureus strain ISP479C and of an isogenic variant (strain PS767) in which sraP had been disrupted by allelic replacement. Platelet binding in vitro by PS767 was 47% ± 17% (mean ± standard deviation) lower than that of ISP479C (P < 0.001). In addition, a recombinant fragment of SraP containing srr1 and the nonrepeat region was found to bind platelets directly. Binding was saturable, suggesting a receptor-ligand interaction. When tested in a rabbit model of endocarditis, in which each animal was simultaneously infected with ISP479C and PS767 at a ratio of approximately 1:1, the titers of the mutant strain within vegetations were significantly lower than those of the parent strain at 1 and 24 h postinfection. These results indicate that SraP can mediate the direct binding of S. aureus to platelets and that the platelet-binding domain of this glycoprotein is located within its N-terminal region. Moreover, the expression of SraP appears to be a virulence determinant in endovascular infection.

* Corresponding author. Mailing address: Division of Infectious Diseases, VA Medical Center (111W), 4150 Clement St., San Francisco, CA 94121. Phone: (415) 221-4810, ext. 2550. Fax: (415) 750-0502. E-mail: sullam{at}itsa.ucsf.edu.

Editor: V. J. DiRita

Infection and Immunity, April 2005, p. 2273-2280, Vol. 73, No. 4
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.4.2273-2280.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Mistou, M.-Y., Dramsi, S., Brega, S., Poyart, C., Trieu-Cuot, P. (2009). Molecular Dissection of the secA2 Locus of Group B Streptococcus Reveals that Glycosylation of the Srr1 LPXTG Protein Is Required for Full Virulence. J. Bacteriol. 191: 4195-4206 [Abstract] [Full Text]  
  • Bensing, B. A., Sullam, P. M. (2009). Characterization of Streptococcus gordonii SecA2 as a Paralogue of SecA. J. Bacteriol. 191: 3482-3491 [Abstract] [Full Text]  
  • Zhu, L., Inoue, K., Yoshizumi, S., Kobayashi, H., Zhang, Y., Ouyang, M., Kato, F., Sugai, M., Inouye, M. (2009). Staphylococcus aureus MazF Specifically Cleaves a Pentad Sequence, UACAU, Which Is Unusually Abundant in the mRNA for Pathogenic Adhesive Factor SraP. J. Bacteriol. 191: 3248-3255 [Abstract] [Full Text]  
  • Zhou, M., Wu, H. (2009). Glycosylation and biogenesis of a family of serine-rich bacterial adhesins. Microbiology 155: 317-327 [Abstract] [Full Text]  
  • Zhou, M., Peng, Z., Fives-Taylor, P., Wu, H. (2008). A Conserved C-Terminal 13-Amino-Acid Motif of Gap1 Is Required for Gap1 Function and Necessary for the Biogenesis of a Serine-Rich Glycoprotein of Streptococcus parasanguinis. Infect. Immun. 76: 5624-5631 [Abstract] [Full Text]  
  • Urano-Tashiro, Y., Yajima, A., Takashima, E., Takahashi, Y., Konishi, K. (2008). Binding of the Streptococcus gordonii DL1 Surface Protein Hsa to the Host Cell Membrane Glycoproteins CD11b, CD43, and CD50. Infect. Immun. 76: 4686-4691 [Abstract] [Full Text]  
  • Siboo, I. R., Chaffin, D. O., Rubens, C. E., Sullam, P. M. (2008). Characterization of the Accessory Sec System of Staphylococcus aureus. J. Bacteriol. 190: 6188-6196 [Abstract] [Full Text]  
  • Bu, S., Li, Y., Zhou, M., Azadin, P., Zeng, M., Fives-Taylor, P., Wu, H. (2008). Interaction between Two Putative Glycosyltransferases Is Required for Glycosylation of a Serine-Rich Streptococcal Adhesin. J. Bacteriol. 190: 1256-1266 [Abstract] [Full Text]  
  • Samen, U., Eikmanns, B. J., Reinscheid, D. J., Borges, F. (2007). The Surface Protein Srr-1 of Streptococcus agalactiae Binds Human Keratin 4 and Promotes Adherence to Epithelial HEp-2 Cells. Infect. Immun. 75: 5405-5414 [Abstract] [Full Text]  
  • Chen, Q., Sun, B., Wu, H., Peng, Z., Fives-Taylor, P. M. (2007). Differential Roles of Individual Domains in Selection of Secretion Route of a Streptococcus parasanguinis Serine-Rich Adhesin, Fap1. J. Bacteriol. 189: 7610-7617 [Abstract] [Full Text]  
  • Bensing, B. A., Siboo, I. R., Sullam, P. M. (2007). Glycine Residues in the Hydrophobic Core of the GspB Signal Sequence Route Export toward the Accessory Sec Pathway. J. Bacteriol. 189: 3846-3854 [Abstract] [Full Text]  
  • Wu, H., Zeng, M., Fives-Taylor, P. (2007). The Glycan Moieties and the N-Terminal Polypeptide Backbone of a Fimbria-Associated Adhesin, Fap1, Play Distinct Roles in the Biofilm Development of Streptococcus parasanguinis. Infect. Immun. 75: 2181-2188 [Abstract] [Full Text]  
  • Sibbald, M. J. J. B., Ziebandt, A. K., Engelmann, S., Hecker, M., de Jong, A., Harmsen, H. J. M., Raangs, G. C., Stokroos, I., Arends, J. P., Dubois, J. Y. F., van Dijl, J. M. (2006). Mapping the Pathways to Staphylococcal Pathogenesis by Comparative Secretomics. Microbiol. Mol. Biol. Rev. 70: 755-788 [Abstract] [Full Text]  
  • Seifert, K. N., Adderson, E. E., Whiting, A. A., Bohnsack, J. F., Crowley, P. J., Brady, L. J. (2006). A unique serine-rich repeat protein (Srr-2) and novel surface antigen ({varepsilon}) associated with a virulent lineage of serotype III Streptococcus agalactiae.. Microbiology 152: 1029-1040 [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»