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Infection and Immunity, September 1998, p. 4274-4282, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Deletion of the Central Proline-Rich Repeat Domain Results in Altered Antigenicity and Lack of Surface Expression of the Streptococcus mutans P1 Adhesin Molecule

L. J. Brady,* D. G. Cvitkovitch,dagger C. M. Geric, M. N. Addison, J. C. Joyce, P. J. Crowley, and A. S. Bleiweis

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

Received 5 December 1997/Returned for modification 20 February 1998/Accepted 8 June 1998

Members of the family of surface adhesins of oral streptococci, including P1 of Streptococcus mutans, contain two highly conserved repeat domains, one rich in alanine (A region) and the other rich in proline (P region). To assess the contribution of the P region to the biological properties of P1, an internal deletion in spaP was engineered. In addition, the P region was subcloned and expressed as a fusion partner with the maltose binding protein of Escherichia coli and liberated by digestion with factor Xa. Results of Western blot experiments in which recombinant polypeptides were probed with a panel of 11 monoclonal antibodies indicated that the P region is a necessary component of conformational epitopes within the central portion of P1. Antibodies reactive with the P region were detected in a polyclonal rabbit antiserum generated against whole S. mutans cells but not in two rabbit antisera generated against purified P1 (Mr ~ 185,000), suggesting that this domain is immunogenic on the surface of intact bacteria but not as part of a soluble full-length molecule. Finally, transformation of a spaP-negative mutant with a shuttle vector containing an internally deleted spaP lacking P-region DNA resulted in a complete absence of surface-localized P1 and substantially less P1 in sonicated cells compared to the case for the mutant complemented with the full-length gene. These results suggest that the P region is an integral component contributing to the conformation of the central region of P1 and indicate that its presence is necessary for surface expression of the molecule on S. mutans.

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

dagger Present address: University of Toronto Dental Research Institute, Toronto, Ontario, Canada M5G 1G6.

Infection and Immunity, September 1998, p. 4274-4282, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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