Imperial College London
Portrait Picture

Professor Neil Fairweather

Faculty of Natural Sciences, Department of Life Sciences

Emeritus Professor
 
 
 
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Contact

 

+44 (0)20 7594 5247n.fairweather

 
 
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Location

 

1.44Flowers buildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Peltier:2017:10.1038/s41598-017-08322-1,
author = {Peltier, J and Shaw, HA and wren, B and Fairweather, NF},
doi = {10.1038/s41598-017-08322-1},
journal = {Scientific Reports},
title = {Disparate subcellular location 1 of putative sortase substrates in Clostridium difficile},
url = {http://dx.doi.org/10.1038/s41598-017-08322-1},
volume = {7},
year = {2017}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - 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.
AU  - Peltier,J
AU  - Shaw,HA
AU  - wren,B
AU  - Fairweather,NF
DO  - 10.1038/s41598-017-08322-1
PY  - 2017///
SN  - 2045-2322
TI  - Disparate subcellular location 1 of putative sortase substrates in Clostridium difficile
T2  - Scientific Reports
UR  - http://dx.doi.org/10.1038/s41598-017-08322-1
UR  - http://hdl.handle.net/10044/1/50089
VL  - 7
ER  -
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