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Infection and Immunity, August 2004, p. 4680-4688, Vol. 72, No. 8
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.8.4680-4688.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Characterization of the Streptococcus mutans P1 Epitope Recognized by Immunomodulatory Monoclonal Antibody 6-11A

Nikki R. Rhodin,1 Jenny M. Cutalo,2,3 Kenneth B. Tomer,2 William P. McArthur,1 and L. Jeannine Brady1*

Department of Oral Biology, College of Dentistry, University of Florida, Gainesville, Florida 32610-0424,1 Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, North Carolina 27709,2 Dental Research Center, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina 275993

Received 9 March 2004/ Returned for modification 12 April 2004/ Accepted 13 May 2004

Monoclonal antibody (MAb) 6-11A directed against Streptococcus mutans surface adhesin P1 was shown previously to influence the mucosal immunogenicity of this organism in BALB/c mice. The specificity of anti-P1 serum immunoglobulin G (IgG) and secretory IgA antibodies and the subclass distribution of anti-P1 serum IgG antibodies were altered, and the ability of elicited serum antibodies to inhibit S. mutans adherence in vitro was in certain cases increased. MAb 6-11A is known to recognize an epitope dependent on the presence of the proline-rich region of the protein, although it does not bind directly to the isolated P-region domain. In this report, we show that MAb 6-11A recognizes a complex discontinuous epitope that requires the simultaneous presence of the alanine-rich repeat domain (A-region) and the P-region. Formation of the core epitope requires the interaction of these segments of P1. Residues amino terminal to the A-region also contributed to recognition by MAb 6-11A but were not essential for binding. Characterization of the MAb 6-11A epitope will enable insight into potential mechanisms of immunomodulation and broaden our understanding of the tertiary structure of P1.

* Corresponding author. Mailing address: Department of Oral Biology, P.O. Box 100424, University of Florida, Gainesville, FL 32610-0424. Phone: (352) 846-0785. Fax: (352) 392-7357. E-mail: jbrady{at}dental.ufl.edu.

Editor: J. D. Clements

Infection and Immunity, August 2004, p. 4680-4688, Vol. 72, No. 8
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.8.4680-4688.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Robinette, R. A., Oli, M. W., McArthur, W. P., Brady, L. J. (2009). Beneficial Immunomodulation by Streptococcus mutans Anti-P1 Monoclonal Antibodies Is Fc Independent and Correlates with Increased Exposure of a Relevant Target Epitope. J. Immunol. 183: 4628-4638 [Abstract] [Full Text]  
  • Crowley, P. J., Seifert, T. B., Isoda, R., van Tilburg, M., Oli, M. W., Robinette, R. A., McArthur, W. P., Bleiweis, A. S., Brady, L. J. (2008). Requirements for Surface Expression and Function of Adhesin P1 from Streptococcus mutans. Infect. Immun. 76: 2456-2468 [Abstract] [Full Text]  
  • Oli, M. W., Rhodin, N., McArthur, W. P., Brady, L. J. (2004). Redirecting the Humoral Immune Response against Streptococcus mutans Antigen P1 with Monoclonal Antibodies. Infect. Immun. 72: 6951-6960 [Abstract] [Full Text]  


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