Saturation mutagenesis of lysine 12 leads to the identification of derivatives of nisin A with enhanced antimicrobial activity

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dc.contributor.authorMolloy, Evelyn M.
dc.contributor.authorField, Des
dc.contributor.authorO'Connor, Paula M.
dc.contributor.authorCotter, Paul D.
dc.contributor.authorHill, Colin
dc.contributor.authorRoss, R. Paul
dc.contributor.funderIrish Governmenten
dc.contributor.funderIrish Research Council for Science Engineering and Technologyen
dc.contributor.funderEnterprise Irelanden
dc.contributor.funderScience Foundation Irelanden
dc.date.accessioned2016-02-17T11:46:19Z
dc.date.available2016-02-17T11:46:19Z
dc.date.issued2013
dc.description.abstractIt is becoming increasingly apparent that innovations from the "golden age'' of antibiotics are becoming ineffective, resulting in a pressing need for novel therapeutics. The bacteriocin family of antimicrobial peptides has attracted much attention in recent years as a source of potential alternatives. The most intensively studied bacteriocin is nisin, a broad spectrum lantibiotic that inhibits Gram-positive bacteria including important food pathogens and clinically relevant antibiotic resistant bacteria. Nisin is gene-encoded and, as such, is amenable to peptide bioengineering, facilitating the generation of novel derivatives that can be screened for desirable properties. It was to this end that we used a site-saturation mutagenesis approach to create a bank of producers of nisin A derivatives that differ with respect to the identity of residue 12 (normally lysine; K12). A number of these producers exhibited enhanced bioactivity and the nisin A K12A producer was deemed of greatest interest. Subsequent investigations with the purified antimicrobial highlighted the enhanced specific activity of this modified nisin against representative target strains from the genera Streptococcus, Bacillus, Lactococcus, Enterococcus and Staphylococcus.en
dc.description.sponsorshipIrish Government (National Development Plan (NDP)); Irish Research Council for Science Engineering and Technology (IRCSET); Enterprise Ireland; Science Foundation Ireland (SFI-CSET, SFI Principal Investigator funding)en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleide58530
dc.identifier.citationMolloy EM, Field D, Connor PMO, Cotter PD, Hill C, Ross RP (2013) Saturation Mutagenesis of Lysine 12 Leads to the Identification of Derivatives of Nisin A with Enhanced Antimicrobial Activity. PLoS ONE 8(3): e58530. doi:10.1371/journal.pone.0058530en
dc.identifier.doi10.1371/journal.pone.0058530
dc.identifier.issn1932-6203
dc.identifier.issued3en
dc.identifier.journaltitlePLOS ONEen
dc.identifier.urihttps://hdl.handle.net/10468/2388
dc.identifier.volume8en
dc.language.isoenen
dc.publisherPublic Library of Scienceen
dc.rights© 2013 Molloy et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are crediteden
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectGram positive pathogensen
dc.subjectPrecursor lipid Iien
dc.subjectLantibiotic nisinen
dc.subjectListeria monocytogenesen
dc.subjectLactococcus lactisen
dc.subjectInnate resistanceen
dc.subjectPeptide pisinen
dc.subjectIn vitroen
dc.subjectGeneen
dc.subjectAntibioticsen
dc.titleSaturation mutagenesis of lysine 12 leads to the identification of derivatives of nisin A with enhanced antimicrobial activityen
dc.typeArticle (peer-reviewed)en
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