Abstract
Streptomyces cinnamoneus DSM 40646 produces the Class II lantibiotic cinnamycin which possesses an unusual mechanism of action, binding to the membrane lipid phosphatidylethanolamine (PE) to elicit its antimicrobial activity. A comprehensive analysis of the cinnamycin biosynthetic gene cluster has unveiled a novel mechanism of immunity in which the producing organism methylates its entire complement of PE prior to the onset of cinnamycin production. Deletion of the PE methyl transferase gene cinorf10, or the two-component regulatory system (cinKR) that controls its expression, leads not only to sensitivity to the closely related lantibiotic duramycin, but also abolishes cinnamycin production, presumably reflecting a fail-safe mechanism that serves to ensure that biosynthesis does not occur until immunity has been established.
Highlights
Cinnamycin (Fig. 1a) is a Class II lantibiotic produced by Streptomyces cinnamoneus DSM 40646 (Fig. 1b) and belongs to the wider family of Ribosomally synthesised post-translationally modified Peptides (RiPPs) [2]
It is a potent antibiotic that is active against a broad range of Gram-positive bacteria and possesses an unusual mechanism of action, binding to the membrane amino phospholipid phosphatidylethanolamine (PE; Fig. 1c), a mechanism that is unique to the cinnamycin family of lantibiotics [10]
Consistent with this hypothesis, deletion of cinA from the heterologous gene cluster in S. lividans resulted in loss of PE methyltransferase (PEMT) activity as well as the expected abolition of cinnamycin production; PEMT activity was restored by the exogenous addition of sub-inhibitory concentrations of duramycin (Fig. 8)
Summary
Cinnamycin (Fig. 1a) is a Class II lantibiotic produced by Streptomyces cinnamoneus DSM 40646 (Fig. 1b) and belongs to the wider family of Ribosomally synthesised post-translationally modified Peptides (RiPPs) [2]. It is a member of a small group of related compounds that
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