ArticleMolecular microbiology2021
A clostripain-like protease plays a major role in generating the secretome of enterotoxigenic Bacteroides fragilis.
Article in Molecular microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 17 citations in OpenAlex.
- Outer membrane vesicles secreted byInfection and immunity · 2026Article
- An ubiquitous antibacterial toxin from human gut bacteria engenders neonatal colonization advantage.Nature communications · 2026Article
- Interbacterial warfare in the human gut: insights from Bacteroidales' perspective.Gut microbes · 2025Review
- Lessons from the model gut BacteroidalesJournal of bacteriology · 2025Review
- A Bacteroides fragilis protease activates host PARCell host & microbe · 2025Article
- Outer Membrane Vesicles FromJournal of extracellular biology · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Identification of a secreted protease frombioRxiv : the preprint server for biology · 2025Article
- Role of E-cadherin in epithelial barrier dysfunction: implications for bacterial infection, inflammation, and disease pathogenesis.Frontiers in cellular and infection microbiology · 2025Review
- Distant relatives of a eukaryotic cell-specific toxin family evolved a complement-like mechanism to kill bacteria.Nature communications · 2024Article
- A proteolytically activated antimicrobial toxin encoded on a mobile plasmid of Bacteroidales induces a protective response.Nature communications · 2022Article
- Article
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4 authors at 1 institution in 1 country.
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Abstract
Bacteroides fragilis toxin (BFT) is a protein secreted by enterotoxigenic (ETBF) strains of B. fragilis. BFT is synthesized as a proprotein (proBFT) that is predicted to be a lipoprotein and that is cleaved into two discrete fragments by a clostripain-like protease called fragipain (Fpn). In this study, we obtained evidence that Fpn cleaves proBFT following its transport across the outer membrane. Remarkably, we also found that the disruption of the fpn gene led to a strong reduction in the level of >100 other proteins, many of which are predicted to be lipoproteins, in the culture medium of an ETBF strain. Experiments performed with purified Fpn provided direct evidence that the protease releases at least some of these proteins from the cell surface. The observation that wild-type cells outcompeted an fpn- strain in co-cultivation assays also supported the notion that Fpn plays an important role in cell physiology and is not simply dedicated to toxin biogenesis. Finally, we found that purified Fpn altered the adhesive properties of HT29 intestinal epithelial cells. Our results suggest that Fpn is a broad-spectrum protease that not only catalyzes the protein secretion on a wide scale but that also potentially cleaves host cell proteins during colonization.
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