Lipid specific nisin activity

Wiedemann I, Breukink E, van Kraaij C, Kuipers OP, Bierbaum G, de Kruijff B, Sahl HG. Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. 

In conclusion, pore formation in the cytoplasmic membrane seems to be a common mode of action of those LAB bacteriocins for which the mode of action has been determined. Some of the class II bacteriocins (lactococcin A, B, G and lactacin F) require a specific receptor molecule for adsorption, whereas nisin also acts on Hposomes and exerts a receptor-independent action. Differences between narrow or wide host-range bacteriocins seem to be correlated with this aspect of a specific receptor, needed for activity. However, which bacteriocin domains confer binding specificities to lipid, protein, or reactive groups remain to be elucidated. 

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