IRIS publication 160749152
Studies with bioengineered Nisin peptides highlight the broad-spectrum potency of Nisin V
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TY - JOUR - Field, D,Quigley, L,O'Connor, PM,Rea, MC,Daly, K,Cotter, PD,Hill, C,Ross, RP - 2010 - January - Microbial Biotechnology - Studies with bioengineered Nisin peptides highlight the broad-spectrum potency of Nisin V - Validated - () - RESISTANT STAPHYLOCOCCUS-AUREUS PRECURSOR LIPID-II MOLECULAR EPIDEMIOLOGIC ANALYSIS GRAM-POSITIVE PATHOGENS LACTIC-ACID BACTERIA LISTERIA-MONOCYTOGENES IN-VITRO LANTIBIOTIC LACTICIN-3147 CLOSTRIDIUM-DIFFICILE STREPTOCOCCUS-MUTANS - 3 - 473 - 486 - 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. - DOI 10.1111/j.1751-7915.2010.00184.x DA - 2010/01 ER -
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@article{V160749152, = {Field, D and Quigley, L and O'Connor, PM and Rea, MC and Daly, K and Cotter, PD and Hill, C and Ross, RP }, = {2010}, = {January}, = {Microbial Biotechnology}, = {Studies with bioengineered Nisin peptides highlight the broad-spectrum potency of Nisin V}, = {Validated}, = {()}, = {RESISTANT STAPHYLOCOCCUS-AUREUS PRECURSOR LIPID-II MOLECULAR EPIDEMIOLOGIC ANALYSIS GRAM-POSITIVE PATHOGENS LACTIC-ACID BACTERIA LISTERIA-MONOCYTOGENES IN-VITRO LANTIBIOTIC LACTICIN-3147 CLOSTRIDIUM-DIFFICILE STREPTOCOCCUS-MUTANS}, = {3}, pages = {473--486}, = {{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.}}, = {DOI 10.1111/j.1751-7915.2010.00184.x}, source = {IRIS} }
Data as stored in IRIS
AUTHORS | Field, D,Quigley, L,O'Connor, PM,Rea, MC,Daly, K,Cotter, PD,Hill, C,Ross, RP | ||
YEAR | 2010 | ||
MONTH | January | ||
JOURNAL_CODE | Microbial Biotechnology | ||
TITLE | Studies with bioengineered Nisin peptides highlight the broad-spectrum potency of Nisin V | ||
STATUS | Validated | ||
TIMES_CITED | () | ||
SEARCH_KEYWORD | RESISTANT STAPHYLOCOCCUS-AUREUS PRECURSOR LIPID-II MOLECULAR EPIDEMIOLOGIC ANALYSIS GRAM-POSITIVE PATHOGENS LACTIC-ACID BACTERIA LISTERIA-MONOCYTOGENES IN-VITRO LANTIBIOTIC LACTICIN-3147 CLOSTRIDIUM-DIFFICILE STREPTOCOCCUS-MUTANS | ||
VOLUME | 3 | ||
ISSUE | |||
START_PAGE | 473 | ||
END_PAGE | 486 | ||
ABSTRACT | 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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DOI_LINK | DOI 10.1111/j.1751-7915.2010.00184.x | ||
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