|Title||Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis.|
|Publication Type||Journal Article|
|Year of Publication||2005|
|Authors||Ekkelenkamp, M. B., M. Hanssen, S-T. D. Hsu, A. de Jong, D. Milatovic, J. Verhoef, and N. A. J. van Nuland|
|Date Published||2005 Mar 28|
|Keywords||Amino Acid Sequence, Anti-Bacterial Agents, Bacteriocins, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Peptides, Protein Processing, Post-Translational, Protein Structure, Tertiary, Staphylococcus epidermidis|
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.
|Alternate Journal||FEBS Lett.|