dipa, a pore-forming protein in the outer membrane of lyme disease spirochetes exhibits specificity for the permeation of dicarboxylatesdipa,成孔的外膜蛋白莱姆病螺旋体展品特异性dicarboxylates渗透的.pdfVIP

DipA, a Pore-Forming Protein in the Outer Membrane of Lyme Disease Spirochetes Exhibits Specificity for the Permeation of Dicarboxylates 1 2. 2. 1 1,3 ¨ 2 Marcus Thein , Mari Bonde , Ignas Bunikis , Katrin Denker , Albert Sickmann , Sven Bergstrom , Roland Benz1,4* ¨ ¨ ˚ 1 Rudolf-Virchow-Center, DFG-Research Center for Experimental Biomedicine, University of Wurzburg, Wurzburg, Germany, 2 Department of Molecular Biology, Umea ˚ ¨ University, Umea, Sweden, 3 Department of Bioanalytics, Leibniz-Institut fur Analytische Wissenschaften – ISAS, Dortmund, Germany, 4 School of Engineering and Science, Jacobs University Bremen, Bremen, Germany Abstract Lyme disease Borreliae are highly dependent on the uptake of nutrients provided by their hosts. Our study describes the identification of a 36 kDa protein that functions as putative dicarboxylate-specific porin in the outer membrane of Lyme disease Borrelia. The protein was purified by hydroxyapatite chromatography from Borrelia burgdorferi B31 and designated as DipA, for dicarboxylate-specific porin A. DipA was partially sequenced, and corresponding genes were identified in the genomes of B. burgdorferi B31, Borrelia garinii PBi and Borrelia afzelii PKo. DipA exhibits high homology to the Oms38 porins of relapsing fever Borreliae. B. burgdorferi DipA was characterized using the black lipid bilayer assay. The protein has a single- channel co