ArticleJournal of bacteriology2003
Identification of secretion determinants of the Bordetella pertussis BrkA autotransporter.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Microbial GAIN domains undergo autoproteolysis and enable release of diverse cell-surface-associated proteins.Current biology : CB · 2026Article
- Advancements in Escherichia coli secretion systems for enhanced recombinant protein production.World journal of microbiology & biotechnology · 2025Review
- Virulence Associated Gene 8 ofFrontiers in immunology · 2018Article
- Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria.Microbiology spectrum · 2015Review
- Secretome of obligate intracellular Rickettsia.FEMS microbiology reviews · 2015Review
- Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.Molecular microbiology · 2015Review
- An alternative outer membrane secretion mechanism for an autotransporter protein lacking a C-terminal stable core.Molecular microbiology · 2013Article
- Probing the applicability of autotransporter based surface display with the EstA autotransporter of Pseudomonas stutzeri A15.Microbial cell factories · 2012Article
- Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Residues in a conserved α-helical segment are required for cleavage but not secretion of an Escherichia coli serine protease autotransporter passenger domain.Journal of bacteriology · 2011Article
- A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocation.The Journal of biological chemistry · 2010Article
- Crystallographic characterization of the passenger domain of the Bordetella autotransporter BrkA.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Virulence factor secretion and translocation by Bordetella species.Current opinion in microbiology · 2009Review
- Highly attenuated Bordetella pertussis strain BPZE1 as a potential live vehicle for delivery of heterologous vaccine candidates.Infection and immunity · 2008Article
- Requirement for YaeT in the outer membrane assembly of autotransporter proteins.Journal of bacteriology · 2007Article
- Role of the alpha-helical linker of the C-terminal translocator in the biogenesis of the serine protease subfamily of autotransporters.Infection and immunity · 2006Article
- Polar localization of the autotransporter family of large bacterial virulence proteins.Journal of bacteriology · 2006Article
- Surface display of proteins by gram-negative bacterial autotransporters.Microbial cell factories · 2006Article
- Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter.The EMBO journal · 2006Article
- The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation.Journal of bacteriology · 2006Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The autotransporters comprise a functionally diverse family of gram-negative proteins that mediate their own export across the bacterial outer membrane. They consist of an amino-terminal passenger region called the "alpha-domain" and the structural hallmark of the autotransporter family, a carboxy-terminal transporter region usually referred to as the "beta-domain." The passenger region can be quite diverse and constitutes the effector functions of these proteins, whereas the C-terminal region is conserved and is responsible for translocating the passenger moiety across the outer membrane. BrkA is the 103-kDa autotransporter protein in Bordetella pertussis that is cleaved to yield a 73-kDa N-terminal alpha-domain and a 30-kDa C-terminal beta-domain. We have previously shown that a recombinant form of the beta-domain of BrkA is capable of forming channels in artificial membranes. Here, we define two additional secretion determinants of BrkA. N-terminal sequencing of the 73-kDa BrkA passenger from B. pertussis and Escherichia coli revealed that BrkA has a 42-amino-acid signal peptide. In addition, deletion analysis of BrkA identified a 31- to 39-amino-acid region found immediately upstream of the beta-domain that was essential for surface expression. This 31- to 39-amino-acid linker region, together with the beta-domain, defines the minimal BrkA translocation unit. The linker region may also serve to anchor the BrkA passenger to the bacterial surface.
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