ArticleBMC microbiology2014
Clostridium difficile has a single sortase, SrtB, that can be inhibited by small-molecule inhibitors.
Article in BMC microbiology, 2014. 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, 30 citations in OpenAlex.
- A sequence invariable region in TcdB2 is required for toxin escape fromJournal of bacteriology · 2024Article
- Rising prevalence and drug resistance ofFrontiers in cellular and infection microbiology · 2024Review
- Sortase-encoding genes,Frontiers in microbiology · 2024Article
- The WalRK Two-Component System Is Essential for Proper Cell Envelope Biogenesis in Clostridioides difficile.Journal of bacteriology · 2022Article
- The divergent roles of sortase in the biology of Gram-positive bacteria.Cell surface (Amsterdam, Netherlands) · 2021Review
- Extracellular DNA, cell surface proteins and c-di-GMP promote biofilm formation in Clostridioides difficile.Scientific reports · 2021Article
- Functional analysis ofThe Journal of biological chemistry · 2020Article
- Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family.The Journal of biological chemistry · 2018Article
- Disparate subcellular location of putative sortase substrates in Clostridium difficile.Scientific reports · 2017Article
- Characteristics of the Clostridium difficile cell envelope and its importance in therapeutics.Microbial biotechnology · 2017Review
- Structural Insights into Substrate Recognition byFrontiers in cellular and infection microbiology · 2016Article
- Cyclic diGMP regulates production of sortase substrates of Clostridium difficile and their surface exposure through ZmpI protease-mediated cleavage.The Journal of biological chemistry · 2015Article
- Structure and function of a Clostridium difficile sortase enzyme.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundBacterial sortases are transpeptidases that covalently anchor surface proteins to the peptidoglycan of the Gram-positive cell wall. Sortase protein anchoring is mediated by a conserved cell wall sorting signal on the anchored protein, comprising of a C-terminal recognition sequence containing an "LPXTG-like" motif, followed by a hydrophobic domain and a positively charged tail.
resultsWe report that Clostridium difficile strain 630 encodes a single sortase (SrtB). A FRET-based assay was used to confirm that recombinant SrtB catalyzes the cleavage of fluorescently labelled peptides containing (S/P)PXTG motifs. Strain 630 encodes seven predicted cell wall proteins with the (S/P)PXTG sorting motif, four of which are conserved across all five C. difficile lineages and include potential adhesins and cell wall hydrolases. Replacement of the predicted catalytic cysteine residue at position 209 with alanine abolishes SrtB activity, as does addition of the cysteine protease inhibitor MTSET to the reaction. Mass spectrometry reveals the cleavage site to be between the threonine and glycine residues of the (S/P)PXTG peptide. Small-molecule inhibitors identified through an in silico screen inhibit SrtB enzymatic activity to a greater degree than MTSET.
conclusionsThese results demonstrate for the first time that C. difficile encodes a single sortase enzyme, which cleaves motifs containing (S/P)PXTG in-vitro. The activity of the sortase can be inhibited by mutation of a cysteine residue in the predicted active site and by small-molecule inhibitors.
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