Source:http://linkedlifedata.com/resource/pubmed/id/21255345
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2011-1-24
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pubmed:abstractText |
Nisin A is the most thoroughly investigated member of the lantibiotic family of antimicrobial peptides. In addition to a long history of safe use as a food antimicrobial, its activity against multi-drug resistant pathogens has resulted in a renewed interest in applying nisin as a chemotherapeutic to treat bacterial infections. The wealth of Nisin-related information that has been generated has also led to the development of the biotechnological capacity to engineer novel Nisin variants with a view to improving the function and physicochemical properties of this already potent peptide. However, the identification of bioengineered Nisin derivatives with enhanced antimicrobial activity against Gram-positive targets is a recent event. In this study, we created stable producers of the most promising derivatives of Nisin A generated to date [M21V (hereafter Nisin V) and K22T (hereafter Nisin T)] and assessed their potency against a range of drug-resistant clinical, veterinary and food pathogens. Nisin T exhibited increased activity against all veterinary isolates, including streptococci and staphylococci, and against a number of multi-drug resistant clinical isolates including MRSA, but not vancomycin-resistant enterococci. In contrast, Nisin V displayed increased potency against all targets tested including hVISA strains and the hyper-virulent Clostridium difficile ribotype 027 and against important food pathogens such as Listeria monocytogenes and Bacillus cereus. Significantly, this enhanced activity was validated in a model food system against L. monocytogenes. We conclude that Nisin V possesses significant potential as a novel preservative or chemotherapeutic compound.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1751-7915
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pubmed:author | |
pubmed:copyrightInfo |
© 2010 The Authors. Journal compilation © 2010 Society for Applied Microbiology and Blackwell Publishing Ltd.
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pubmed:issnType |
Electronic
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
473-86
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pubmed:meshHeading |
pubmed-meshheading:21255345-Amino Acid Substitution,
pubmed-meshheading:21255345-Anti-Bacterial Agents,
pubmed-meshheading:21255345-Bacteriocins,
pubmed-meshheading:21255345-Gram-Positive Bacteria,
pubmed-meshheading:21255345-Microbial Sensitivity Tests,
pubmed-meshheading:21255345-Microbial Viability,
pubmed-meshheading:21255345-Nisin
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pubmed:year |
2010
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pubmed:articleTitle |
Studies with bioengineered Nisin peptides highlight the broad-spectrum potency of Nisin V.
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pubmed:affiliation |
Department of Microbiology, University College Cork, Cork, Ireland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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