ArticleJournal of bacteriology1999
The C-terminal domain of the Bordetella pertussis autotransporter BrkA forms a pore in lipid bilayer membranes.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Bordetella pertussis autotransporter Vag8 binds human C1 esterase inhibitor and confers serum resistance.PloS one · 2011Article
- Highly attenuated Bordetella pertussis strain BPZE1 as a potential live vehicle for delivery of heterologous vaccine candidates.Infection and immunity · 2008Article
- The autodisplay story, from discovery to biotechnical and biomedical applications.Microbiology and molecular biology reviews : MMBR · 2007Review
- Surface display of proteins by gram-negative bacterial autotransporters.Microbial cell factories · 2006Article
- Type V protein secretion pathway: the autotransporter story.Microbiology and molecular biology reviews : MMBR · 2004Review
- Strain-dependent role of BrkA during Bordetella pertussis infection of the murine respiratory tract.Infection and immunity · 2004Article
- Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter.The EMBO journal · 2004Article
- Structure of the translocator domain of a bacterial autotransporter.The EMBO journal · 2004Article
- Molecular basis of bacterial outer membrane permeability revisited.Microbiology and molecular biology reviews : MMBR · 2003Review
- Identification of secretion determinants of the Bordetella pertussis BrkA autotransporter.Journal of bacteriology · 2003Article
- Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains.The EMBO journal · 2002Article
- Translocation of a functional protein by a voltage-dependent ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- The Haemophilus influenzae Hia adhesin is an autotransporter protein that remains uncleaved at the C terminus and fully cell associated.Journal of bacteriology · 2000Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.