The Staphylococcus epidermidis derived epidermin was the first lantibiotic that has been shown to be ribosomally synthesized and posttranslationally modified. Together with gallidermin, produced by Staphylococcus gallinarum, they belong to the large class of cationic antimicrobial peptides (CAMPs) that act against a broad spectrum of Gram-positive bacteria. Here we describe the genetic organization, biosynthesis and modification, excretion, extracellular activation of the modified pre-peptide by proteolytic processing, self-protection of the producer, gene regulation, structure, and the mode of action of gallidermin and epidermin. We also address mechanisms of bacterial tolerance to these lantibiotics and other CAMPs. Particularly gallidermin has a high potential for therapeutic application, as it is active against methicillin-resistant Staphylococcus aureus strains (MRSA) and as it is able to prevent biofilm formation at sublethal concentrations.
Keywords: (Z)-2,3-didehydrobutyrine; 2,3-didehydroalanine; 3-methyllanthionine; AviCys; Dha; Dhb; Epidermin; Gallidermin; Lan; Lantibiotics; MeLan; S-[(Z)-2-aminovinyl]-d-cysteine; Staphylococcus; lanthionine.
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