Nisin resistance

Gasson MJ (1984) Transfer of sucrose fermenting ability, nisin resistance and nisin production in Streptococcus lactis 712. FEMS Microbiol Lett 21 7-10... 

Froseth BR, Herman RE, McKay LL (1988) Cloning of nisin resistance determinant and replication origin on 7.6-kilobase EcoRI fragment of pNP40 from Streptococcus lactis subsp. diacetylactis DRC3. Appl Environ Microbiol 54 2136-2139... 

Froseth BR, McKay LL (1991) Molecular characterization of the nisin resistance region of Lactococcus lactis subsp. lactis biovar diacetylactis DRC3. Appl Environ Microbiol 57 804-811... 

Daeschel MA, ]ung D-S, Watson BT Controlling wine malolaccic fermentation with nisin and nisin-resistant strains of Leuconosioc oenos. Appl Environ Microbiol 1991 57 601-603. 

Like lysozyme, nisin is an effective inhibitor of Gram-positive bacteria. Radler (1990a 1990b) determined that most lactic acid bacteria are inhibited by nisin, even in low concentrations, while alcoholic fermentation was not affected. However, the author reported that species varied in their response, with L. casei being the least sensitive. Daeschel et al. (1991) successfully used nisin-resistant strains of O. oeni to conduct MLF in a wine previously treated with nisin to control other spoilage bacteria. Others have reported that nisin killed 100% of O. oeni present as a biofilm on stainless steel (Nel et ak, 2002). Despite its potential, nisin is not currently approved for use in wine in the United States. 

Daeschel, M.A., D.-S.Jung, and B.T. Watson. 1991. Controlling wine malolactic fermentation with nisin and nisin-resistant strains of Leuconostoc oenos. Appl. Environ. Microbiol. 57 601—603. 

Mazzotta, A. S., Modi, K. and Montville, T. J., 2000. Nisin-resistant Listeria monocytogenes and Nisin-resistant Clostridium botulinum are not resistant to common food preservatives. J Food Science 65, 888-893. 

Crandall, A.D. and Montville, T.J. (1998). Nisin resistance in Listeria monocytogenes ATCC 700302 is a complex phenotype. Appl Environ Microbiol 64, 231-237. 

Ming, X.T. and Daeschel, M.A. (1993). Nisin Resistance of Eoodbome bacteria and the specific resistance responses of Listeria rrwnocytogenes Scott-A. J Food Prot 56, 944—948. 

Sun, Z., Zhong, J., liang, X., et al. (2009). Novel mechanism for nisin resistance via proteolytic degradation of nisin by the nisin resistance protein NSR. Antimicrob Agents Chemother 53, 1964-1973. 

Verheul, A., Russell, N.J., VantHof, R., et al. (1997). Modifications of membrane phospholipid composition in nisin-resistant Listeria manacytagenes Scott A. Appl Enviran Micrabial 63, 3451-3457. 

Potential therapeutic applications of host defense peptides also include the lantibiotic nisin. Indeed, nisin has had an impressive history as a food preservative with FDA approval in 1988 for use in pasteurized, processed cheese spreads. The attractiveness of nisin as a potential therapeutic is also enhanced due to its relative resistance to proteases and broad spectrum Gram-positive antimicrobial activity including multidrug-resistant strains. Biosynexus Inc. has licensed the use of nisin for human clinical applications and Immucell Corp. has licensed the use of Mast Out, an antimastitic nisin-containing product, to Pfizer Animal Health." Indeed, nisin formulations have been used as an active agent in the topical therapies Mast Out and Wipe-Out for bovine mastitis, an inflammatory disorder of the udder that is the most persistent disease in dairy cows." ... 

Replacement of Dha by Dhb and vice versa has been reported for several lantibiotics. Replacement of Ser at position 5 by Thr led to the production of Dhb instead of Dha in mature nisin The mutant exhibited increased resistance to chemical degradation, but this was accompanied by a 2- to 10-fold reduction in bioactivity toward various indicator strains. In contrast, replacement of Dha at position 2 in nisin Z with Dhb resulted in a mutant that was twice as active as native nisin Z. ° The gallidermin variant Dhbl4Dha did not exhibit any noticeable decrease in activity, ° and the DhblODha mutant of mutacin II also showed similar activity as wild type. " The promiscuity of the biosynthetic enzymes is also well illustrated by the production of a nisin mutant with a Dhb residue at position 18 in place of Gly after introduction of a Thr codon in nisA and the analogous introduction of a novel Dha in place of a Lys at position 18 in Pep... 

Research on antibiotics which do not produce multiple resistance is, of course, desirable. Nisin appears to present just such a situation although its applications are narrow. Some feed additives are capable of "curing multiple resistance in enterics (50). This area deserves more research and emphasis. 

The prototypical lantibiotic, nisin, was discovered in 1928 for its antibacterial properties and has been used as a preservative in dairy products since the 1950s (1). Nisin and other lantibiotics exhibit nanomolar efficacy against many Gram-positive strains of bacteria (2), which include methicillin resistant Staphylococcus aureus, vancomycin resistant enterococci, and oxacillin resistant bacteria. On the other hand, some lantibiotics function as morphogenetic peptides rather than antibiotics and are important for spore formation in streptomycetes (3). Since the structural elucidation of nisin in the early 1970s, extensive research efforts have been directed at understanding the biosynthesis and mode of action of various lantibiotics. 

Add the liposomal ingredients to a preheated (60°C, 5 min) mixture of nisin (200 pg/ml) and a polyol such as glycerol (final concentration 3%, v/v) in a heat-resistant flask such as a pyrex beaker. Alternatively, a heat-resistant bottle with six baffles can be used as explained and pictured in reference (49). 

Elevated temperature and citric acid have been found to increase the susceptibility to nisin, both in culture and in foods. Exposure to a temperature of 60°C for 10 min, followed by 24 h incubation by 30°C showed no survival of bacterial cells. However, at a temperature of 50°C some viable cells were found with the application of nisin, but survivor numbers were significantly reduced. Stationary phase cells are more resistant to both organic acids alone, as well as in combination with nisin, than log-phase cells. It is speculated that Gram-negative bacterial cells are protected from the effects of nisin by the composition of their outer layers. When these are weakened by elevated temperature, they become sensitive by similar mechanisms as Gram-positive bacteria (Phillips and Duggan, 2002). 

Consumer resistance to the use of synthetic additives in foods has stimulated interest in natural additives and preservatives. The principal natural additive used in cheese is the bacteriocin, nisin. Bacteriocins are peptides which inhibit a limited range of bacteria, usually closely related to the producer organism. The potential of nisin, produced by Lactococcus lactis, as a food preservative was first demonstrated using nisin-producing cultures in the manufacturer of Swiss-type cheese to prevent spoilage by Clostridia (Hirsch et ai, 1951). To date, nisin is the only purified bacteriocin commercially exploited as a food preservative. It can be added to processed cheese products to prevent late blowing by Clostridia, the spores of which, if present in the natural cheese, survive pasteurization (Barnby-Smith, 1992). 

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