ArticleScientific reports2015
Structure and function of a Clostridium difficile sortase enzyme.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Rising prevalence and drug resistance ofFrontiers in cellular and infection microbiology · 2024Review
- Article
- The divergent roles of sortase in the biology of Gram-positive bacteria.Cell surface (Amsterdam, Netherlands) · 2021Review
- The C-Terminal Domain of Clostridioides difficile TcdC Is Exposed on the Bacterial Cell Surface.Journal of bacteriology · 2020Article
- Functional analysis ofThe Journal of biological chemistry · 2020Article
- Quercetin impairs Streptococcus pneumoniae biofilm formation by inhibiting sortase A activity.Journal of cellular and molecular medicine · 2018Article
- Disparate subcellular location of putative sortase substrates in Clostridium difficile.Scientific reports · 2017Article
- Pilus biogenesis of Gram-positive bacteria: Roles of sortases and implications for assembly.Protein science : a publication of the Protein Society · 2017Review
- Structure and specificity of a new class of CaThe Journal of biological chemistry · 2017Article
- Sortase Transpeptidases: Structural Biology and Catalytic Mechanism.Advances in protein chemistry and structural biology · 2017Review
- 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
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Sortase enzymes are responsible for covalent anchoring of specific proteins to the peptidoglycan of the cell wall of gram-positive bacteria. In some gram-positive bacteria (e.g. Staphylococcus aureus), sortases have been found to be essential for pathogenesis and their inhibitors are under development as potential novel therapeutics. Here we provide the first report on the structural characterisation of the C. difficile sortase. An active site mutant was crystallised and its structure determined to 2.55 Å by X-ray diffraction to provide structural insight into its catalytic mechanism. In order to elucidate the role of the sortase in the cell wall biogenesis, a C. difficile sortase knockout strain was constructed by intron mutagenesis. Characterisation of this mutant led to the discovery that the putative adhesin CD0386 is anchored to the peptidoglycan of C. difficile by the sortase SrtB and that an SPKTG peptide motif is involved in the transpeptidation reaction with the C. difficile peptidoglycan. In an animal model for C. difficile infection, the SrtB mutant caused disease at a similar rate of onset as the wild type strain. In conclusion, our detailed study shows that the SrtB enzyme from C. difficile does not play an essential role in pathogenesis.
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Registered trials
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.