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

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dc.contributor.author Molloy, Evelyn M.
dc.contributor.author Field, Des
dc.contributor.author O'Connor, Paula M.
dc.contributor.author Cotter, Paul D.
dc.contributor.author Hill, Colin
dc.contributor.author Ross, R. Paul
dc.date.accessioned 2016-02-17T11:46:19Z
dc.date.available 2016-02-17T11:46:19Z
dc.date.issued 2013
dc.identifier.citation Molloy 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.0058530 en
dc.identifier.volume 8 en
dc.identifier.issued 3 en
dc.identifier.issn 1932-6203
dc.identifier.uri http://hdl.handle.net/10468/2388
dc.identifier.doi 10.1371/journal.pone.0058530
dc.description.abstract It 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.sponsorship Irish 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.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher Public Library of Science en
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 credited en
dc.rights.uri http://creativecommons.org/licenses/by/4.0/ en
dc.subject Gram positive pathogens en
dc.subject Precursor lipid Ii en
dc.subject Lantibiotic nisin en
dc.subject Listeria monocytogenes en
dc.subject Lactococcus lactis en
dc.subject Innate resistance en
dc.subject Peptide pisin en
dc.subject In vitro en
dc.subject Gene en
dc.subject Antibiotics en
dc.title Saturation mutagenesis of lysine 12 leads to the identification of derivatives of nisin A with enhanced antimicrobial activity en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Colin Hill, Microbiology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: c.hill@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.internal.wokid WOS:000316251100061
dc.contributor.funder Irish Government en
dc.contributor.funder Irish Research Council for Science Engineering and Technology en
dc.contributor.funder Enterprise Ireland en
dc.contributor.funder Science Foundation Ireland en
dc.description.status Peer reviewed en
dc.identifier.journaltitle PLOS ONE en
dc.internal.IRISemailaddress c.hill@ucc.ie en
dc.identifier.articleid e58530


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© 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 credited Except where otherwise noted, this item's license is described as © 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 credited
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