Improved lanthipeptide detection and prediction for antiSMASH

PLoS One. 2014 Feb 20;9(2):e89420. doi: 10.1371/journal.pone.0089420. eCollection 2014.

Abstract

Lanthipeptides are a class of ribosomally synthesised and post-translationally modified peptide (RiPP) natural products from the bacterial secondary metabolism. Their name is derived from the characteristic lanthionine or methyl-lanthionine residues contained in the processed peptide. Lanthipeptides that possess an antibacterial activity are called lantibiotics. Whereas multiple tools exist to identify lanthipeptide gene clusters from genomic data, no programs are available to predict the post-translational modifications of lanthipeptides, such as the proteolytic cleavage of the leader peptide part or tailoring modifications based on the analysis of the gene cluster sequence. antiSMASH is a software pipeline for the identification of secondary metabolite biosynthetic clusters from genomic input and the prediction of products produced by the identified clusters. Here we present a novel antiSMASH module using a rule-based approach to combine signature motifs for biosynthetic enzymes and lanthipeptide-specific cleavage site motifs to identify lanthipeptide clusters in genomic data, assign the specific lanthipeptide class, predict prepeptide cleavage, tailoring reactions, and the processed molecular weight of the mature peptide products.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / analysis*
  • Bacteriocins / analysis*
  • Bacteriocins / genetics
  • Molecular Sequence Data
  • Multigene Family
  • Peptide Fragments / analysis*
  • Protein Processing, Post-Translational
  • Software*

Substances

  • Anti-Bacterial Agents
  • Bacteriocins
  • Peptide Fragments

Grants and funding

Funding was provided by the German Ministry of Education and Research (BMBF) (Grant 0315585A to TW), German Centre for Infection Research (DZIF) (8000-402-2 to TW and WW), LAPTOP (Grant 245066 to WW). Funding for open access charge: Deutsche Forschungsgemeinschaft (DFG) and Open Access Publishing Fund of Tübingen University. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.