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pubmed-article:10482528pubmed:abstractTextBrkA 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.lld:pubmed
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pubmed-article:10482528pubmed:authorpubmed-author:ShannonJ LJLlld:pubmed
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pubmed-article:10482528pubmed:articleTitleThe C-terminal domain of the Bordetella pertussis autotransporter BrkA forms a pore in lipid bilayer membranes.lld:pubmed
pubmed-article:10482528pubmed:affiliationDepartment of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3.lld:pubmed
pubmed-article:10482528pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10482528pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:10482528pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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