TP0453, a Concealed Outer Membrane Protein of Treponema pallidum , Enhances Membrane Permeability
| Autor: | Carson J. La Vake, Robert Brasseur, Morgan E. La Vake, Marc Decaffmeyer, Karsten R. O. Hazlett, Esther J. Robinson, Kenneth W. Bourell, Michael P. Bennett, Justin D. Radolf, David L. Cox, Daniel C. Desrosiers |
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| Rok vydání: | 2005 |
| Předmět: |
Cell Membrane Permeability
Membrane permeability Translocase of the outer membrane Peripheral membrane protein Biology Enzymes and Proteins Microbiology Transmembrane protein Biochemistry Antigens Surface Biophysics Outer membrane efflux proteins Virulence-related outer membrane protein family Treponema pallidum Bacterial outer membrane Molecular Biology Integral membrane protein Bacterial Outer Membrane Proteins |
| Zdroj: | Journal of Bacteriology. 187:6499-6508 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.187.18.6499-6508.2005 |
| Popis: | 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 β-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 β-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 α-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. |
| Databáze: | OpenAIRE |
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