The two peptide lantibiotic lacticin 3147 acts synergistically with polymyxin to inhibit Gram negative bacteria

Hdl Handle:
http://hdl.handle.net/10147/302697
Title:
The two peptide lantibiotic lacticin 3147 acts synergistically with polymyxin to inhibit Gram negative bacteria
Authors:
Draper, Lorraine A; Cotter, Paul D; Hill, Colin; Ross, R P
Citation:
BMC Microbiology. 2013 Sep 26;13(1):212
Issue Date:
26-Sep-2013
URI:
http://dx.doi.org/10.1186/1471-2180-13-212; http://hdl.handle.net/10147/302697
Abstract:
Abstract Background The emergence of bacterial drug resistance encourages the re-evaluation of the potential of existing antimicrobials. Lantibiotics are post-translationally modified, ribosomally synthesised antimicrobial peptides with a broad spectrum antimicrobial activity. Here, we focussed on expanding the potential of lacticin 3147, one of the most studied lantibiotics and one which possesses potent activity against a wide range of Gram positive species including many nosocomial pathogens. More specifically, our aim was to investigate if lacticin 3147 activity could be enhanced when combined with a range of different clinical antibiotics. Results Initial screening revealed that polymyxin B and polymyxin E (colistin) exhibited synergistic activity with lacticin 3147. Checkerboard assays were performed against a number of strains, including both Gram positive and Gram negative species. The resultant fractional inhibitory concentration (FIC) index values established that, while partial synergy was detected against Gram positive targets, synergy was obvious against Gram negative species, including Cronobacter and E. coli. Conclusions Combining lacticin 3147 with low levels of a polymyxin could provide a means of broadening target specificity of the lantibiotic, while also reducing polymyxin use due to the lower concentrations required as a result of synergy.
Item Type:
Article
Language:
en
Keywords:
COMMUNICABLE DISEASE; INFECTION CONTROL

Full metadata record

DC FieldValue Language
dc.contributor.authorDraper, Lorraine Aen_GB
dc.contributor.authorCotter, Paul Den_GB
dc.contributor.authorHill, Colinen_GB
dc.contributor.authorRoss, R Pen_GB
dc.date.accessioned2013-10-04T13:23:37Z-
dc.date.available2013-10-04T13:23:37Z-
dc.date.issued2013-09-26-
dc.identifier.citationBMC Microbiology. 2013 Sep 26;13(1):212en_GB
dc.identifier.urihttp://dx.doi.org/10.1186/1471-2180-13-212-
dc.identifier.urihttp://hdl.handle.net/10147/302697-
dc.description.abstractAbstract Background The emergence of bacterial drug resistance encourages the re-evaluation of the potential of existing antimicrobials. Lantibiotics are post-translationally modified, ribosomally synthesised antimicrobial peptides with a broad spectrum antimicrobial activity. Here, we focussed on expanding the potential of lacticin 3147, one of the most studied lantibiotics and one which possesses potent activity against a wide range of Gram positive species including many nosocomial pathogens. More specifically, our aim was to investigate if lacticin 3147 activity could be enhanced when combined with a range of different clinical antibiotics. Results Initial screening revealed that polymyxin B and polymyxin E (colistin) exhibited synergistic activity with lacticin 3147. Checkerboard assays were performed against a number of strains, including both Gram positive and Gram negative species. The resultant fractional inhibitory concentration (FIC) index values established that, while partial synergy was detected against Gram positive targets, synergy was obvious against Gram negative species, including Cronobacter and E. coli. Conclusions Combining lacticin 3147 with low levels of a polymyxin could provide a means of broadening target specificity of the lantibiotic, while also reducing polymyxin use due to the lower concentrations required as a result of synergy.-
dc.language.isoenen
dc.subjectCOMMUNICABLE DISEASEen_GB
dc.subjectINFECTION CONTROLen_GB
dc.titleThe two peptide lantibiotic lacticin 3147 acts synergistically with polymyxin to inhibit Gram negative bacteriaen_GB
dc.typeArticleen
dc.language.rfc3066en-
dc.rights.holderLorraine A Draper et al.; licensee BioMed Central Ltd.-
dc.description.statusPeer Reviewed-
dc.date.updated2013-10-02T04:20:01Z-
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