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Journal of Bacteriology, December 2002, p. 6811-6819, Vol. 184, No. 24
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.24.6811-6819.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Elimination of Channel-Forming Activity by Insertional Inactivation of the p13 Gene in Borrelia burgdorferi

Yngve Östberg,1 Marija Pinne,1 Roland Benz,2 Patricia Rosa,3 and Sven Bergström1*

Department of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden,1 Lehrstuhl für Biotechnologie, Biozentrum der Universität Würzburg, D-97074 Würzburg, Germany,2 Laboratory of Human Bacterial Pathogenesis, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 598403

Received 8 July 2002/ Accepted 11 September 2002

P13 is a chromosomally encoded 13-kDa integral outer membrane protein of the Lyme disease agent, Borrelia burgdorferi. The aim of this study was to investigate the function of the P13 protein. Here, we inactivated the p13 gene by targeted mutagenesis and investigated the porin activities of outer membrane proteins by using lipid bilayer experiments. Channel-forming activity was lost in the p13 mutant compared to wild-type B. burgdorferi, indicating that P13 may function as a porin. We purified native P13 to homogeneity by fast performance liquid chromatography and demonstrated that pure P13 has channel-forming activity with a single-channel conductance in 1 M KCl of 3.5 nS, the same as the porin activity that was lost in the p13 mutant. Further characterization of the channel formed by P13 suggested that it is cation selective and voltage independent. In addition, no major physiological effects of the inactivated p13 gene could be detected under normal growth conditions. The inactivation of p13 is the first reported inactivation of a gene encoding an integral outer membrane protein in B. burgdorferi. Here, we describe both genetic and biophysical experiments indicating that P13 in B. burgdorferi is an outer membrane protein with porin activity.

* Corresponding author. Mailing address: Department of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden. Phone: (46-90)-785 6726. Fax: (46-90)-772630. E-mail: sven.bergstrom{at}molbiol.umu.se.

Journal of Bacteriology, December 2002, p. 6811-6819, Vol. 184, No. 24
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.24.6811-6819.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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