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Identification and characterisation of capidermicin, a novel bacteriocin produced by Staphylococcus capitis

One hundred human-derived coagulase negative staphylococci (CoNS) were screened for antimicrobial activity using agar-based deferred antagonism assays with a range of indicator bacteria. Based on the findings of the screen and subsequent well assays with cell free supernatants and whole cell extract...

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Detalles Bibliográficos
Autores principales: Lynch, David, O’Connor, Paula M., Cotter, Paul D., Hill, Colin, Field, Des, Begley, Máire
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6795431/
https://www.ncbi.nlm.nih.gov/pubmed/31618225
http://dx.doi.org/10.1371/journal.pone.0223541
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author Lynch, David
O’Connor, Paula M.
Cotter, Paul D.
Hill, Colin
Field, Des
Begley, Máire
author_facet Lynch, David
O’Connor, Paula M.
Cotter, Paul D.
Hill, Colin
Field, Des
Begley, Máire
author_sort Lynch, David
collection PubMed
description One hundred human-derived coagulase negative staphylococci (CoNS) were screened for antimicrobial activity using agar-based deferred antagonism assays with a range of indicator bacteria. Based on the findings of the screen and subsequent well assays with cell free supernatants and whole cell extracts, one strain, designated CIT060, was selected for further investigation. It was identified as Staphylococcus capitis and herein we describe the purification and characterisation of the novel bacteriocin that the strain produces. This bacteriocin which we have named capidermicin was extracted from the cell-free supernatant of S. capitis CIT060 and purified to homogeneity using reversed-phase high performance liquid chromatography (RP-HPLC). Matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometric (MS) analysis revealed that the capidermicin peptide has a mass of 5,464 Da. Minimal inhibitory concentration (MIC) experiments showed that capidermicin was active in the micro-molar range against all the Gram-positive bacteria that were tested. Antimicrobial activity was retained over a range of pHs (2–11) and temperatures (10–121°C x 15 mins). The draft genome sequence of S. capitis CIT060 was determined and the genes predicted to be involved in the biosynthesis of capidermicin were identified. These genes included the predicted capidermicin precursor gene, and genes that are predicted to encode a membrane transporter, an immunity protein and a transcriptional regulator. Homology searches suggest that capidermicin is a novel member of the family of class II leaderless bacteriocins.
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spelling pubmed-67954312019-10-20 Identification and characterisation of capidermicin, a novel bacteriocin produced by Staphylococcus capitis Lynch, David O’Connor, Paula M. Cotter, Paul D. Hill, Colin Field, Des Begley, Máire PLoS One Research Article One hundred human-derived coagulase negative staphylococci (CoNS) were screened for antimicrobial activity using agar-based deferred antagonism assays with a range of indicator bacteria. Based on the findings of the screen and subsequent well assays with cell free supernatants and whole cell extracts, one strain, designated CIT060, was selected for further investigation. It was identified as Staphylococcus capitis and herein we describe the purification and characterisation of the novel bacteriocin that the strain produces. This bacteriocin which we have named capidermicin was extracted from the cell-free supernatant of S. capitis CIT060 and purified to homogeneity using reversed-phase high performance liquid chromatography (RP-HPLC). Matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometric (MS) analysis revealed that the capidermicin peptide has a mass of 5,464 Da. Minimal inhibitory concentration (MIC) experiments showed that capidermicin was active in the micro-molar range against all the Gram-positive bacteria that were tested. Antimicrobial activity was retained over a range of pHs (2–11) and temperatures (10–121°C x 15 mins). The draft genome sequence of S. capitis CIT060 was determined and the genes predicted to be involved in the biosynthesis of capidermicin were identified. These genes included the predicted capidermicin precursor gene, and genes that are predicted to encode a membrane transporter, an immunity protein and a transcriptional regulator. Homology searches suggest that capidermicin is a novel member of the family of class II leaderless bacteriocins. Public Library of Science 2019-10-16 /pmc/articles/PMC6795431/ /pubmed/31618225 http://dx.doi.org/10.1371/journal.pone.0223541 Text en © 2019 Lynch et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Lynch, David
O’Connor, Paula M.
Cotter, Paul D.
Hill, Colin
Field, Des
Begley, Máire
Identification and characterisation of capidermicin, a novel bacteriocin produced by Staphylococcus capitis
title Identification and characterisation of capidermicin, a novel bacteriocin produced by Staphylococcus capitis
title_full Identification and characterisation of capidermicin, a novel bacteriocin produced by Staphylococcus capitis
title_fullStr Identification and characterisation of capidermicin, a novel bacteriocin produced by Staphylococcus capitis
title_full_unstemmed Identification and characterisation of capidermicin, a novel bacteriocin produced by Staphylococcus capitis
title_short Identification and characterisation of capidermicin, a novel bacteriocin produced by Staphylococcus capitis
title_sort identification and characterisation of capidermicin, a novel bacteriocin produced by staphylococcus capitis
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6795431/
https://www.ncbi.nlm.nih.gov/pubmed/31618225
http://dx.doi.org/10.1371/journal.pone.0223541
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