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Journal of Bacteriology, December 2003, p. 6860-6869, Vol. 185, No. 23
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.23.6860-6869.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Two Paralogous Families of a Two-Gene Subtilisin Operon Are Widely Distributed in Oral Treponemes

Frederick F. Correia,1 Alvin R. Plummer,1 Richard P. Ellen,2 Chris Wyss,3 Susan K. Boches,1 Jamie L. Galvin,1 Bruce J. Paster,1,4 and Floyd E. Dewhirst1,4*

Department of Molecular Genetics, The Forsyth Institute, Boston, Massachusetts 02115,1 CIHR Group in Matrix Dynamics, University of Toronto, Toronto, Canada M5G 1G6,2 Institut für Orale Mikrobiologie und Allgemeine Immunologie, Universität Zürich, CH-8028 Zürich, Switzerland,3 Department of Oral and Developmental Biology, Harvard School of Dental Medicine, Boston, Massachusetts 021154

Received 9 May 2003/ Accepted 2 September 2003

Certain oral treponemes express a highly proteolytic phenotype and have been associated with periodontal diseases. The periodontal pathogen Treponema denticola produces dentilisin, a serine protease of the subtilisin family. The two-gene operon prcA-prtP is required for expression of active dentilisin (PrtP), a putative lipoprotein attached to the treponeme's outer membrane or sheath. The purpose of this study was to examine the diversity and structure of treponemal subtilisin-like proteases in order to better understand their distribution and function. The complete sequences of five prcA-prtP operons were determined for Treponema lecithinolyticum, "Treponema vincentii," and two canine species. Partial operon sequences were obtained for T. socranskii subsp. 04 as well as 450- to 1,000-base fragments of prtP genes from four additional treponeme strains. Phylogenetic analysis demonstrated that the sequences fall into two paralogous families. The first family includes the sequence from T. denticola. Treponemes possessing this operon family express chymotrypsin-like protease activity and can cleave the substrate N-succinyl-alanyl-alanyl-prolyl-phenylalanine-p-nitroanilide (SAAPFNA). Treponemes possessing the second paralog family do not possess chymotrypsin-like activity or cleave SAAPFNA. Despite examination of a range of protein and peptide substrates, the specificity of the second protease family remains unknown. Each of the fully sequenced prcA and prtP genes contains a 5' hydrophobic leader sequence with a treponeme lipobox. The two paralogous families of treponeme subtilisins represent a new subgroup within the subtilisin family of proteases and are the only subtilisin lipoprotein family. The present study demonstrated that the subtilisin paralogs comprising a two-gene operon are widely distributed among treponemes.

* Corresponding author. Mailing address: Department of Molecular Genetics The Forsyth Institute, 140 The Fenway, Boston, MA 02115. Phone: (617) 456-7708. Fax: (617) 456-7737. E-mail: fdewhirst{at}forsyth.org.

Journal of Bacteriology, December 2003, p. 6860-6869, Vol. 185, No. 23
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.23.6860-6869.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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