Disparate subcellular location of putative sortase substrates in Clostridium difficile.

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 Rep

journal_title

Scientific reports

authors

Peltier J,Shaw HA,Wren BW,Fairweather NF

doi

10.1038/s41598-017-08322-1

subject

Has Abstract

pub_date

2017-08-23 00:00:00

pages

9204

issue

1

issn

2045-2322

pii

10.1038/s41598-017-08322-1

journal_volume

7

pub_type

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