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Journal of Bacteriology, September 2005, p. 6499-6508, Vol. 187, No. 18
0021-9193/05/$08.00+0     doi:10.1128/JB.187.18.6499-6508.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

TP0453, a Concealed Outer Membrane Protein of Treponema pallidum, Enhances Membrane Permeability

Karsten R. O. Hazlett,1* David L. Cox,4 Marc Decaffmeyer,6 Michael P. Bennett,5 Daniel C. Desrosiers,1 Carson J. La Vake,1 Morgan E. La Vake,1 Kenneth W. Bourell,1 Esther J. Robinson,7,{dagger} Robert Brasseur,6 and Justin D. Radolf1,2,3

Center for Microbial Pathogenesis,1 Departments of Medicine,2 Genetics and Developmental Biology, University of Connecticut Health Center, Farmington, Connecticut 06030,3 Division of STD Laboratory Research, Centers for Disease Control and Prevention, Atlanta, Georgia 30333,4 Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269,5 Centre de Biophysique Moléculaire Numérique FSAGX, 5030 Gembloux, Belgium,6 and Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, Texas 753907

Received 20 April 2005/ Accepted 5 July 2005

The outer membrane of Treponema pallidum, the noncultivable agent of venereal syphilis, contains a paucity of protein(s) which has yet to be definitively identified. In contrast, the outer membranes of gram-negative bacteria contain abundant immunogenic membrane-spanning ß-barrel proteins mainly involved in nutrient transport. The absence of orthologs of gram-negative porins and outer membrane nutrient-specific transporters in the T. pallidum genome predicts that nutrient transport across the outer membrane must differ fundamentally in T. pallidum and gram-negative bacteria. Here we describe a T. pallidum outer membrane protein (TP0453) that, in contrast to all integral outer membrane proteins of known structure, lacks extensive ß-sheet structure and does not traverse the outer membrane to become surface exposed. TP0453 is a lipoprotein with an amphiphilic polypeptide containing multiple membrane-inserting, amphipathic {alpha}-helices. Insertion of the recombinant, nonlipidated protein into artificial membranes results in bilayer destabilization and enhanced permeability. Our findings lead us to hypothesize that TP0453 is a novel type of bacterial outer membrane protein which may render the T. pallidum outer membrane permeable to nutrients while remaining inaccessible to antibody.

* Corresponding author. Mailing address: Center for Microbial Pathogenesis, University of Connecticut Health Center, 263 Farmington Ave., Farmington, CT 06030. Phone: (860) 679-8391. Fax: (860) 679-1358. E-mail: KHazlett{at}up.uchc.edu.

{dagger} Retired.

Journal of Bacteriology, September 2005, p. 6499-6508, Vol. 187, No. 18
0021-9193/05/$08.00+0     doi:10.1128/JB.187.18.6499-6508.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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