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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, Robert Brasseur,⁶ and Justin D. Radolf^1,2,3

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 -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.

Retired.

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