[en] he outer membrane of Treponema pallidum, the non-cultivable 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 beta-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 beta-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, non-lipidated 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Hazlett, Kro.
Cox, Dl.
Decaffmeyer, Marc ; Université de Liège - ULiège > Gembloux Agro-Bio Tech
Bennett, Mp.
Desrosiers, Dc.
La Vake, Cj.
La Vake, Me.
Bourell, Kw.
Robinson, Ej.
Brasseur, Robert ; Université de Liège - ULiège > Gembloux Agro-Bio Tech
Radolf, Jd.
Language :
English
Title :
Tp0453, A Concealed Outer Membrane Protein Of Treponema Pallidum, Enhances Membrane Permeability
Publication date :
2005
Journal title :
Journal of Bacteriology
ISSN :
0021-9193
eISSN :
1098-5530
Publisher :
American Society for Microbiology, Washington, United States - District of Columbia
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