Identification and characterization of a bioactive lantibiotic produced by Staphylococcus warneri

Jørgen Petersen, Anders Boysen, Lotte Fogh, Kathrine Tabermann, Thomas Kofoed, Angus King, Petra Schrotz-King, Martin Christian Hansen

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Lantibiotics are a group of potent antibacterial agents that contain unusual amino acids, such as the thioether amino acids lanthionine and methyllanthionine, and the didehydroamino acids didehydroalanine and didehydro-aminobutyric acid. Here, we report on an antibacterial lantibiotic peptide named SWLP1 (Staphylococcus warneri lantibiotic peptide 1), which is secreted from Staphylococcus warneri (deposited with DSMZ, accession number DSM 16081). SWLP1 was purified from growth media. The purified peptide displays antibacterial activity against several species, including Staphylococcus epidermidis. The molecular mass of SWLP1 is 2998.9 Da as determined by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. The sequence and possible structure was elucidated by combining electrospray ionization mass spectrometry/mass spectrometry data of ethanethiol-treated and non-ethanethiol-treated tryptic fragments of the SWLP1. SWLP1 contains three thioether bridges, one didehydroalanine, and three didehydroaminobutyric acids. This peptide has the potential to be used in treatment of several Gram-positive bacterial infections.
Original languageEnglish
JournalBiological Chemistry
Volume390
Issue number5-6
Pages (from-to)437-44
Number of pages8
ISSN1431-6730
DOIs
Publication statusPublished - 2009

Keywords

  • Amino Acid Sequence
  • Anti-Bacterial Agents
  • Bacteriocins
  • Enterococcus faecium
  • Klebsiella pneumoniae
  • Molecular Sequence Data
  • Spectrometry, Mass, Electrospray Ionization
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Staphylococcus
  • Staphylococcus epidermidis

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