Isolation of a new epidermin variant from two strains of Staphylococcus epidermidis--frequency of lantibiotic production in coagulase-negative staphylococci.
A novel lantibiotic identified during the screening of 187 coagulase-negative staphylococci, has been structurally characterised. (Val1, Leu6)-epidermin was purified from culture supernatants of two Staphylococcus epidermidis strains, BN-V1 and BN-V301 following successive separation by adsorption, cation exchange and C18 reversed-phase chromatography. Separation of the purified peptides by SDS-polyacrylamide gel electrophoresis suggested a molecular mass of ca. 2000 Da and electrospray mass spectrometry subsequently demonstrated that both peptides had a mass of 2151 Da; a mass which is different from that of all previously described antimicrobial peptides. Amino acid analysis showed that both peptides contained lanthionine and were very similar to epidermin, while automated N-terminal sequencing by Edman degradation confirmed the identity of the two peptides as a natural variant of the antimicrobial lantibiotic epidermin, and demonstrated the conservative amino acid exchanges in positions one and six.