The potency of the broad spectrum bacteriocin, bactofencin A, against staphylococci is highly dependent on primary structure, N-terminal charge and disulphide formation

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dc.contributor.author O'Connor, Paula M.
dc.contributor.author O'Shea, Eileen F.
dc.contributor.author Cotter, Paul D.
dc.contributor.author Hill, Colin
dc.contributor.author Ross, R. Paul
dc.date.accessioned 2018-09-27T12:08:24Z
dc.date.available 2018-09-27T12:08:24Z
dc.date.issued 2018
dc.identifier.citation O’ Connor, P. M., O’ Shea, E. F., Cotter, P. D., Hill, C. and Ross, R. P. (2018) 'The potency of the broad spectrum bacteriocin, bactofencin A, against staphylococci is highly dependent on primary structure, N-terminal charge and disulphide formation', Scientific Reports, 8(1), 11833 (8pp). doi: 10.1038/s41598-018-30271-6 en
dc.identifier.volume 8
dc.identifier.startpage 1
dc.identifier.endpage 8
dc.identifier.issn 2045-2322
dc.identifier.uri http://hdl.handle.net/10468/6946
dc.identifier.doi 10.1038/s41598-018-30271-6
dc.description.abstract Bactofencin A is a novel class IId bacteriocin, produced by the intestinal isolate Lactobacillus salivarius DPC6502, which has potent activity against medically significant pathogens including Staphylococcus aureus. This bacteriocin is unusual in that it has a highly cationic N terminus and a single disulfide bond between Cys7 and Cys22, resulting in a large C terminal loop. In this study, a library of synthetic bactofencin A variants were screened against the mastitis isolate, S. aureus DPC5246, to identify key residues responsible for activity. It was apparent that substituting either cysteine of the disulfide bond with either serine or alanine significantly reduced the activity of the bacteriocin, confirming the importance of the C terminal loop. Substituting N terminal amino acids with alanine had no effect on activity, whereas sequential removal of the N terminal positively charged residues resulted in an increasingly inactive peptide. A complete (synthetic) alanine scanning analysis revealed that the residues between Val9 and Gly17 were most affected by substitution suggesting that this area has a major influence on the potency of the bacteriocin. Substituting residues in the loop region between Cys7 and Cys22 for D-amino acid equivalents had a more detrimental effect on activity than L-alanine substitutions. Specifically Y10A, N11A, P15A and T16A are active at 4, 16, 1 and 16 μM respectively while their D equivalents were inactive at 1000 μM, the highest concentration tested. Ultimately, this study identifies the critical features in the primary structure of the bacteriocin which gives it such potent activity against pathogenic staphylococci. en
dc.description.sponsorship Department of Agriculture, Fisheries and Food (Food Institutional Research Measure (04/R&D/C/232) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher Springer Nature en
dc.relation.uri https://www.nature.com/articles/s41598-018-30271-6
dc.rights © 2018, the Authors. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. en
dc.rights.uri http://creativecommons.org/licenses/by/4.0/
dc.subject Lactobacillus salivarius en
dc.subject Amino acid en
dc.subject Pathogenic staphylococci en
dc.subject N terminal en
dc.title The potency of the broad spectrum bacteriocin, bactofencin A, against staphylococci is highly dependent on primary structure, N-terminal charge and disulphide formation en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Paul Ross, College Of Sefs Office, University College Cork, Cork, Ireland. +353-21-490-3000 Email: p.ross@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.contributor.funder Science Foundation Ireland
dc.contributor.funder Department of Agriculture, Food and the Marine
dc.description.status Peer reviewed en
dc.identifier.journaltitle Scientific Reports en
dc.internal.IRISemailaddress p.ross@ucc.ie en
dc.identifier.articleid 11833
dc.relation.project info:eu-repo/grantAgreement/SFI/SFI Research Centres/12/RC/2273/IE/Alimentary Pharmabiotic Centre (APC) - Interfacing Food & Medicine/


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© 2018, the Authors. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. Except where otherwise noted, this item's license is described as © 2018, the Authors. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
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