ArticleMolecular microbiology2012
The prodomain of the Bordetella two-partner secretion pathway protein FhaB remains intracellular yet affects the conformation of the mature C-terminal domain.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- C-terminal domain of the filamentous hemagglutinin FhaB is crucial for interaction ofbioRxiv : the preprint server for biology · 2026Article
- Bacteria deliver a microtubule-binding protein into mammalian cells to promote colonization.Science (New York, N.Y.) · 2026Article
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- Filamentous Hemagglutinin ofInternational journal of molecular sciences · 2022Article
- Secrete or perish: The role of secretion systems inComputational and structural biotechnology journal · 2021Review
- Review
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- Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions.Frontiers in cellular and infection microbiology · 2017Review
- Bordetella adenylate cyclase toxin interacts with filamentous haemagglutinin to inhibit biofilm formation in vitro.Molecular microbiology · 2017Article
- XacFhaB adhesin, an important Xanthomonas citri ssp. citri virulence factor, is recognized as a pathogen-associated molecular pattern.Molecular plant pathology · 2016Article
- Bordetella filamentous hemagglutinin and fimbriae: critical adhesins with unrealized vaccine potential.Pathogens and disease · 2015Review
- Sequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.Protein science : a publication of the Protein Society · 2015Article
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- Review
- System specificity of the TpsB transporters of coexpressed two-partner secretion systems of Neisseria meningitidis.Journal of bacteriology · 2013Article
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Authors and funding
5 authors.
Funding
Abstract
Two-partner secretion (TPS) systems use β-barrel proteins of the Omp85-TpsB superfamily to transport large exoproteins across the outer membranes of Gram-negative bacteria. The Bordetella FHA/FhaC proteins are prototypical of TPS systems in which the exoprotein contains a large C-terminal prodomain that is removed during translocation. Although it is known that the FhaB prodomain is required for FHA function in vivo, its role in FHA maturation has remained mysterious. We show here that the FhaB prodomain is required for the extracellularly located mature C-terminal domain (MCD) of FHA to achieve its proper conformation. We show that the C-terminus of the prodomain is retained intracellularly and that sequences within the N-terminus of the prodomain are required for this intracellular localization. We also identify sequences at the C-terminus of the MCD that are required for release of mature FHA from the cell surface. Our data support a model in which the intracellularly located prodomain affects the final conformation of the extracellularly located MCD. We hypothesize that maturation triggers cleavage and degradation of the prodomain.
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