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Infect. Immun. doi:10.1128/IAI.01424-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

A novel Treponema pallidum antigen, TP0136, is an outer membrane protein that binds human fibronectin

Mary Beth Brinkman, Melanie A. McGill, Jonas Petterson, Arthur Rogers, Petra Matjková, David majs, George M. Weinstock, Steven J. Norris, and Timothy Palzkill^*

Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA; Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, 6431 Fannin Street, Houston, TX 77030, USA; Department of Molecular Virology & Microbiology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA; Department of Microbiology and Molecular Genetics, University of Texas-Houston Medical School, 6431 Fannin Street, Houston, TX 77030, USA; Department of Biology, Faculty of Medicine, Masaryk University, Tomeova 12, 602 00 Brno, Czech Republic; Human Genome Sequencing Center, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA

^* To whom correspondence should be addressed. Email: timothyp{at}bcm.tmc.edu.

	Abstract

The antigenicity, structural location, and function of the predicted lipoprotein TP0136 of Treponema pallidum subsp. pallidum were investigated based on previous screening studies indicating that anti-TP0136 antibodies are present in the sera of syphilis patients and experimentally infected rabbits. Recombinant TP0136 protein (rTP0136) was purified and shown to be strongly antigenic during human and experimental rabbit infection. The TP0136 protein was exposed on the surface of the bacterial outer membrane, and bound to the host extracellular matrix glycoproteins fibronectin and laminin. In addition, the TP0136 open reading frame was shown to be highly polymorphic among T. pallidum subspecies and strains at the nucleotide and amino acid levels. Finally, the ability of rTP0136 protein to act as a protective antigen to subsequent challenge with infectious T. pallidum was assessed in the rabbit model of infection. Immunization with rTP0136 delayed ulceration but did not prevent infection or the formation of lesions. These results demonstrate that TP0136 is expressed on the outer membrane of the treponeme during infection and may be involved in attachment to host extracellular matrix components.