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Infection and Immunity, June 2008, p. 2456-2468, Vol. 76, No. 6
0019-9567/08/$08.00+0     doi:10.1128/IAI.01315-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Requirements for Surface Expression and Function of Adhesin P1 from Streptococcus mutans ^,

Paula J. Crowley, Trevor B. Seifert,^|| Ryutaro Isoda, Marloes van Tilburg,^¶ Monika W. Oli, Rebekah A. Robinette, William P. McArthur, Arnold S. Bleiweis, and L. Jeannine Brady^*

Department of Oral Biology, University of Florida, Gainesville, Florida 32610

Received 28 September 2007/ Returned for modification 30 December 2007/ Accepted 14 March 2008

In this report, we define requirements for the successful translocation and functional maturation of the adhesin P1 of Streptococcus mutans. Conformational epitopes recognized by anti-P1 monoclonal antibodies (MAbs) were further characterized, thus facilitating the use of particular MAbs as tools to monitor the locations of various forms of the protein. We show that correct localization of P1 is dependent on structural features of the molecule itself, including a requisite A region-P region intramolecular interaction that occurs within the cell prior to secretion. P1 also was shown to be affected by several members of the protein-folding-secretion-turnover apparatus. It does not achieve a fully functional form in the absence of the trigger factor PPIase homolog RopA, and its translocation is delayed when DnaK levels are limited. In addition, dnaK message levels are differentially altered in the presence of P1 lacking the alanine-rich compared to the proline-rich repeat domains. Lastly, nonsecreted P1 lacking the P region accumulates within the cell in the absence of htrA, implying an intracellular HtrA protease function in the degradation and turnover of this particular internal-deletion polypeptide. However, the opposite effect is seen for full-length P1, suggesting a sensing mechanism and substrate-dependent alteration in HtrA's function and effect that is consistent with its known ability to switch between chaperone and protease, depending on environmental perturbations.

Published ahead of print on 24 March 2008.

Supplemental material for this article may be found at http://iai.asm.org/.

Editor: V. J. DiRita

^|| Present address: Florida Department of Law Enforcement, Pensacola, FL 32501.

Present address: Department of Oral and Molecular Microbiology, Graduate School of Dentistry, Osaka University, Osaka, Japan 565-0871.

^¶ Deceased.

Present address: Banyan Biomarkers, Inc., Alachua, FL 32615.

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