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. diffi...

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Autores principales: Johann Peltier, Helen A. Shaw, Brendan W. Wren, Neil F. Fairweather
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Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/58afa41b9fab4de785c328b5caf7e816
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spelling oai:doaj.org-article:58afa41b9fab4de785c328b5caf7e8162021-12-02T15:05:43ZDisparate subcellular location of putative sortase substrates in Clostridium difficile10.1038/s41598-017-08322-12045-2322https://doaj.org/article/58afa41b9fab4de785c328b5caf7e8162017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-08322-1https://doaj.org/toc/2045-2322Abstract 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.Johann PeltierHelen A. ShawBrendan W. WrenNeil F. FairweatherNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Johann Peltier
Helen A. Shaw
Brendan W. Wren
Neil F. Fairweather
Disparate subcellular location of putative sortase substrates in Clostridium difficile
description 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.
format article
author Johann Peltier
Helen A. Shaw
Brendan W. Wren
Neil F. Fairweather
author_facet Johann Peltier
Helen A. Shaw
Brendan W. Wren
Neil F. Fairweather
author_sort Johann Peltier
title Disparate subcellular location of putative sortase substrates in Clostridium difficile
title_short Disparate subcellular location of putative sortase substrates in Clostridium difficile
title_full Disparate subcellular location of putative sortase substrates in Clostridium difficile
title_fullStr Disparate subcellular location of putative sortase substrates in Clostridium difficile
title_full_unstemmed Disparate subcellular location of putative sortase substrates in Clostridium difficile
title_sort disparate subcellular location of putative sortase substrates in clostridium difficile
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/58afa41b9fab4de785c328b5caf7e816
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AT helenashaw disparatesubcellularlocationofputativesortasesubstratesinclostridiumdifficile
AT brendanwwren disparatesubcellularlocationofputativesortasesubstratesinclostridiumdifficile
AT neilffairweather disparatesubcellularlocationofputativesortasesubstratesinclostridiumdifficile
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