Bioengineering nisin to overcome the nisin resistance protein

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dc.contributor.authorField, Des
dc.contributor.authorBlake, Tony
dc.contributor.authorMathur, Harsh
dc.contributor.authorO'Connor, Paula M.
dc.contributor.authorCotter, Paul D.
dc.contributor.authorRoss, R. Paul
dc.contributor.authorHill, Colin
dc.contributor.funderScience Foundation Irelanden
dc.date.accessioned2018-12-17T15:03:28Z
dc.date.available2018-12-17T15:03:28Z
dc.date.issued2018-12-11
dc.date.updated2018-12-17T14:51:37Z
dc.description.abstractThe emergence and dissemination of antibiotic resistant bacteria is a major medical challenge. Lantibiotics are highly modified bacterially produced antimicrobial peptides that have attracted considerable interest as alternatives or adjuncts to existing antibiotics. Nisin, the most widely studied and commercially exploited lantibiotic, exhibits high efficacy against many pathogens. However, some clinically relevant bacteria express highly specific membrane‐associated nisin resistance proteins. One notable example is the nisin resistance protein (NSR) that acts by cleaving the peptide bond between ring E and the adjacent serine 29, resulting in a truncated peptide with significantly less activity. We utilised a complete bank of bioengineered nisin (nisin A) producers in which the serine 29 residue has been replaced with every alternative amino acid. The nisin A S29P derivative was found to be as active as nisin A against a variety of bacterial targets but, crucially, exhibited a 20‐fold increase in specific activity against a strain expressing the nisin resistance protein. Another derivative, nisin PV, exhibited similar properties but was much less prone to oxidation. This version of nisin with enhanced resistance to specific resistance mechanisms could prove useful in the fight against antibiotic resistant pathogens.en
dc.description.statusPeer revieweden
dc.description.versionAccepted Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.citationField, D., Blake, T., Mathur, H., O'Connor, P. M., Cotter, P. D., Ross, R. P. and Hill, C. (2018) 'Bioengineering Nisin to overcome the Nisin Resistance Protein', Molecular Microbiology, In Press, doi: 10.1111/mmi.14183en
dc.identifier.doi10.1111/mmi.14183
dc.identifier.endpage36en
dc.identifier.issn0950-382X
dc.identifier.issn1365-2958
dc.identifier.journaltitleMolecular Microbiologyen
dc.identifier.startpage1en
dc.identifier.urihttps://hdl.handle.net/10468/7231
dc.language.isoenen
dc.publisherWileyen
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Technology and Innovation Development Award (TIDA)/14/TIDA/2286/IE/Nis-2-Gen: Developing Second Generation Nisin_s with Therapeutic Applications./en
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Technology and Innovation Development Award (TIDA) - Training Award/10/IN.1/B3027 TIDA Training 11/IE/Lantibiotics: the next generation/en
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Principal Investigator Programme (PI)/11/PI/1137/IE/Obesibiotics/en
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Research Centres/12/RC/2273/IE/Alimentary Pharmabiotic Centre (APC) - Interfacing Food & Medicine/en
dc.relation.urihttps://onlinelibrary.wiley.com/doi/abs/10.1111/mmi.14183
dc.rights© 2018 This article is protected by copyright. All rights reserved. This is the peer reviewed version of the following article: (2018), ‘Bioengineering Nisin to overcome the Nisin Resistance Protein’, Mol Microbiol. Accepted Author Manuscript, which has been published in final form at https://doi.org/10.1111/mmi.14183. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.en
dc.subjectBacterial resistanceen
dc.subjectNisin resistance proteinen
dc.subjectAntimicrobial peptideen
dc.subjectNisinen
dc.subjectLantibioticen
dc.subjectBacteriocinen
dc.titleBioengineering nisin to overcome the nisin resistance proteinen
dc.typeArticle (peer-reviewed)en
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