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dc.contributor.authorO'Shea, Eileen F.*
dc.contributor.authorO'Connor, Paula M.*
dc.contributor.authorCotter, Paul D.*
dc.contributor.authorRoss, R Paul*
dc.contributor.authorHill, Colin*
dc.date.accessioned2012-08-20T16:09:45Z
dc.date.available2012-08-20T16:09:45Z
dc.date.issued25/06/2010
dc.identifier.citationEileen F. O’ Shea, Paula M. O’ Connor, Paul D. Cotter et al. Synthesis of trypsin-resistant variants of the Listeria-active bacteriocin salivaricin P. Appl. Environ. Microbiol. 2010; 76 (16): 5356-5362. DOI: 10.1128/AEM.00523-10en_GB
dc.identifier.issn0099-2240
dc.identifier.urihttp://hdl.handle.net/11019/87
dc.descriptionpeer-revieweden_GB
dc.description.abstractTwo-component Salivaricin P-like bacteriocins have demonstrated potential as antimicrobials capable of controlling infections in the gastrointestinal tract (GIT). The anti-Listeria activity of salivaricin P is optimal when the individual peptides, Sln1 and Sln2, are added in succession in a 1:1 ratio. However, as degradation by digestive proteases may compromise the functionality of these peptides within the GIT we investigated the potential to create salivaricin variants with enhanced resistance to the intestinal protease, trypsin. A total of 11 variants of the salivaricin P components were generated in which conservative modifications at the trypsin-specific cleavage sites were explored in order to protect the peptides from trypsin degradation while maintaining their potent antimicrobial activity. Analysis of these variants revealed that eight were resistant to trypsin digestion while retaining antimicrobial activity. Combining the complementary trypsin resistant variants Sln1-5 and Sln2-3 resulted in a MIC50 of 300 nM against Listeria monocytogenes, a 3.75-fold reduction in activity compared to wild-type salivaricin P. This study demonstrates the potential of engineering bacteriocins variants which are resistant to specific protease action but which retain significant antimicrobial activity.en_GB
dc.description.sponsorshipThis work was funded by the Food Institutional Research Measure of the Department of Agriculture, Fisheries and Food, and the Science Foundation of Ireland funded Centre for Science, Engineering and Technology (SFI-CSET): the Alimentary Pharmabiotic Centreen_GB
dc.language.isoenen_GB
dc.publisherAmerican Society for Microbiologyen_GB
dc.relation.ispartofseriesApplied and Environmental Microbiology;Vol.76
dc.subjectSalivaricin Pen_GB
dc.subjectBacteriocinen_GB
dc.subjectVarianten_GB
dc.subjectTrypsinen_GB
dc.subjectGastrointestinal tracten_GB
dc.titleSynthesis of trypsin-resistant variants of the Listeria-active bacteriocin salivaricin Pen_GB
dc.typeArticleen_GB
dc.identifier.rmis5271
dc.identifier.doihttp://dx.doi.org/10.1128/AEM.00523-10
dc.contributor.sponsorDepartment of Agriculture, Food and the Marine, Ireland
dc.contributor.sponsorScience Foundation Ireland
dc.contributor.sponsorTeagasc Walsh Fellowship Programme
refterms.dateFOA2018-01-12T07:27:49Z


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