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Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis

Publication Type:

Journal Article

Authors:

Ekkelenkamp,M.B.; Hanssen,M.; nny Hsu,S.T.; de,Jong A.; Milatovic,D.; Verhoef,J.; van Nuland,N.A.

Source:

Volume 579, Issue 9, p.1917 - 1922 (2005)

URL:

PM:15792796

Keywords:

Amino Acid Sequence; Anti-Bacterial Agents; chemistry; isolation & purification; Bacteriocins; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Peptides; Protein Processing; Post-Translational; Protein Structure; Tertiary; Staphylococcus epidermidi

Abstract:

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

Notes:

DA - 20050328
IS - 0014-5793 (Print)
LA - eng
PT - Journal Article
RN - 0 (Anti-Bacterial Agents)
RN - 0 (Bacteriocins)
RN - 0 (Peptides)
RN - 0 (epilancin 15X)
SB - IM