Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of 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.
Ekkelenkamp
Miquel B
MB
University Medical Center Utrecht, Utrecht University, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands. M.Ekkelenkamp@lab.azu.nl
Hanssen
Micha
M
Danny Hsu
Shang-Te
ST
de Jong
Ad
A
Milatovic
Dana
D
Verhoef
Jan
J
van Nuland
Nico A J
NA
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000302:isolation & purification; D001430:Bacteriocins; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D013212:Staphylococcus epidermidis / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D010455:Peptides; C500288:epilancin 15X