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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Peltier J,Shaw HA,Wren BW,Fairweather NFdoi
10.1038/s41598-017-08322-1subject
Has Abstractpub_date
2017-08-23 00:00:00pages
9204issue
1issn
2045-2322pii
10.1038/s41598-017-08322-1journal_volume
7pub_type
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