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Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis
Author(s) -
Ekkelenkamp Miquel B.,
Hanssen Micha,
Danny Hsu Shang-Te,
de Jong Ad,
Milatovic Dana,
Verhoef Jan,
van Nuland Nico A.J.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.01.083
Subject(s) - lantibiotics , staphylococcus epidermidis , lanthionine , chemistry , moiety , protein primary structure , peptide , stereochemistry , peptide sequence , biochemistry , bacteriocin , microbiology and biotechnology , bacteria , staphylococcus aureus , biology , antimicrobial , genetics , organic chemistry , gene
The potential application of lantibiotics as food‐preserving agents and more recently as antibiotics has strongly increased the interest in these antibacterial peptides. Here, we report the elucidation of the primary and three‐dimensional structures of the novel lantibiotic epilancin 15X from Staphylococcus epidermidis using high‐resolution nuclear magnetic resonance spectroscopy and tandem mass spectrometry. The molecule contains ten post‐translationally modified amino acids, three lanthionine ring structures and a hydroxy‐propionyl N‐terminal moiety. The primary and tertiary structure and the distribution of positive charges are closely similar to the previously identified lantibiotic epilancin K7, most likely indicative of a common mode of action.