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Journal of Bacteriology, September 1999, p. 5838-5842, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The C-Terminal Domain of the Bordetella pertussis Autotransporter BrkA Forms a Pore in Lipid Bilayer Membranes

Jennifer L. Shannon and Rachel C. Fernandez*

Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3

Received 18 May 1999/Accepted 1 July 1999

BrkA is a 103-kDa outer membrane protein of Bordetella pertussis that mediates resistance to antibody-dependent killing by complement. It is proteolytically processed into a 73-kDa N-terminal domain and a 30-kDa C-terminal domain as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. BrkA is also a member of the autotransporter family of proteins. Translocation of the N-terminal domain of the protein across the outer membrane is hypothesized to occur through a pore formed by the C-terminal domain. To test this hypothesis, we performed black lipid bilayer experiments with purified recombinant protein. The BrkA C-terminal protein showed an average single-channel conductance of 3.0 nS in 1 M KCl. This result strongly suggests that the C-terminal autotransporter domain of BrkA is indeed capable of forming a pore.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, #300-6174 University Blvd., Vancouver, B.C., Canada V6T 1Z3. Phone: (604) 822-6824. Fax: (604) 822-6041. E-mail: rachelf{at}interchange.ubc.ca.

Journal of Bacteriology, September 1999, p. 5838-5842, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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