ArticleScientific reports2017
Disparate subcellular location of putative sortase substrates in Clostridium difficile.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- The divergent roles of sortase in the biology of Gram-positive bacteria.Cell surface (Amsterdam, Netherlands) · 2021Review
- Biofilm regulation in Clostridioides difficile: Novel systems linked to hypervirulence.PLoS pathogens · 2021Review
- Extracellular DNA, cell surface proteins and c-di-GMP promote biofilm formation in Clostridioides difficile.Scientific reports · 2021Article
- Clostridium difficile clade 3 (RT023) have a modified cell surface and contain a large transposable island with novel cargo.Scientific reports · 2019Article
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Authors and funding
4 authors.
Funding
Abstract
Clostridium difficile is a gastrointestinal pathogen but how the bacterium colonises this niche is still little understood. Sortase enzymes covalently attach specific bacterial proteins to the peptidoglycan cell wall and are often involved in colonisation by pathogens. Here we show C. difficile proteins CD2537 and CD3392 are functional substrates of sortase SrtB. Through manipulation of the C-terminal regions of these proteins we show the SPKTG motif is essential for covalent attachment to the cell wall. Two additional putative substrates, CD0183 which contains an SPSTG motif, and CD2768 which contains an SPQTG motif, are not cleaved or anchored to the cell wall by sortase. Finally, using an in vivo asymmetric cleavage assay, we show that despite containing a conserved SPKTG motif, in the absence of SrtB these proteins are localised to disparate cellular compartments.
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