Biochemical, structural, and genetic characterization of tridecaptin A₁, an antagonist of Campylobacter jejuni

Christopher T Lohans, Dr. Marco J van Belkum, Stephen A Cochrane, Dr. Zedu Huang, Dr. Clarissa S Sit, Prof. Lynn M McMullen, Prof. John C Vederas

Research output: Contribution to journalArticle

36 Citations (Scopus)


Bacillus circulans NRRL B-30644 (now Paenibacillus terrae) was previously reported to produce SRCAM 1580, a bacteriocin active against the food pathogen Campylobacter jejuni. We have been unable to isolate SRCAM 1580, and did not find any genetic determinants in the genome of this strain. We now report the reassignment of this activity to the lipopeptide tridecaptin A₁. Structural characterization of tridecaptin A1 was achieved through NMR, MS/MS and GC-MS studies. The structure was confirmed through the first chemical synthesis of tridecaptin A₁, which also revealed the stereochemistry of the lipid chain. The impact of this stereochemistry on antimicrobial activity was examined. The biosynthetic machinery responsible for tridecaptin production was identified through bioinformatic analyses. P. terrae NRRL B-30644 also produces paenicidin B, a novel lantibiotic active against Gram-positive bacteria. MS/MS analyses indicate that this lantibiotic is structurally similar to paenicidin A.

Original languageEnglish
Pages (from-to)243-249
Issue number2
Early online date30 Dec 2013
Publication statusPublished - 24 Jan 2014


  • Amino Acid Sequence
  • Anti-Bacterial Agents
  • Bacteriocins
  • Campylobacter jejuni
  • Lipids
  • Lipopeptides
  • Molecular Sequence Data
  • Multigene Family
  • Paenibacillus
  • Peptides
  • Stereoisomerism
  • Journal Article
  • Research Support, Non-U.S. Gov't

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