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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.date.accessioned2015-01-30T14:01:47Z
dc.date.available2015-01-30T14:01:47Z
dc.date.issued11/03/2013
dc.identifier.citationMolloy EM, Field D, Connor PMO, Cotter PD, Hill C, et al. (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_GB
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/11019/771
dc.descriptionpeer-revieweden_GB
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_GB
dc.description.sponsorshipThis work was supported by the Irish Government under the National Development Plan; by the Irish Research Council for Science Engineering and Technology (IRCSET); by Enterprise Ireland; and by Science Foundation Ireland (SFI), through the Alimentary Pharmabiotic Centre (APC) at University College Cork, Ireland, which is supported by the SFI-funded Centre for Science, Engineering and Technology (SFI-CSET) and provided P.D.C., C.H. and R.P.R. with SFI Principal Investigator funding.
dc.language.isoenen_GB
dc.publisherPLOSen_GB
dc.relation.ispartofseriesPLOS ONE;vol 8
dc.subjectNisin A derivativesen_GB
dc.subjectAntimicrobial activityen_GB
dc.subjectSite-saturation mutagenesisen_GB
dc.subjectGram positive bacteriaen_GB
dc.titleSaturation Mutagenesis of Lysine 12 Leads to the Identification of Derivatives of Nisin A with Enhanced Antimicrobial Activityen_GB
dc.typeArticleen_GB
dc.identifier.rmisMDBY-0106-5271
dc.identifier.doihttp://dx.doi.org/10.1371/journal.pone.0058530
dc.contributor.sponsorIrish Research Council for Science, Engineering and Technology
dc.contributor.sponsorEnterprise Ireland
dc.contributor.sponsorScience Foundation Ireland
refterms.dateFOA2018-01-12T08:22:56Z


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