Lantibiotics: Peptides of diverse structure and function

Research output: Contribution to journalReview article

Abstract

The current need for antibiotics with novel target molecules has coincided with advances in technical approaches for the structural and functional analysis of the lantibiotics, which are ribosomally synthesized peptides produced by gram-positive bacteria. These peptides have antibiotic or morphogenetic activity and are structurally defined by the presence of unusual amino acids introduced by posttranslational modification. Lantibiotics are complex polycyclic molecules formed by the dehydration of select Ser and Thr residues and the intramolecular addition of Cys thiols to the resulting unsaturated amino acids to form lanthionine and methyllanthionine bridges, respectively. Importantly, the structural and functional diversity of the lantibiotics is much broader than previously imagined. Here we discuss this growing collection of molecules and introduce some recendy discovered peptides, review advances in enzymology and protein engineering, and discuss the regulatory networks that govern the synthesis of the lantibiotics by the producing organisms.

Original languageEnglish (US)
Pages (from-to)477-501
Number of pages25
JournalAnnual review of microbiology
Volume61
DOIs
StatePublished - Nov 14 2007

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Bacteriocins
Peptides
Anti-Bacterial Agents
Protein Engineering
Gram-Positive Bacteria
Post Translational Protein Processing
Dehydration
Sulfhydryl Compounds
Amino Acids

Keywords

  • Bacteriocin
  • Peptide antibiotic
  • Peptide engineering
  • Posttranslational modification

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

Lantibiotics : Peptides of diverse structure and function. / Willey, Joanne M.; van der Donk, Wilfred Adrianus.

In: Annual review of microbiology, Vol. 61, 14.11.2007, p. 477-501.

Research output: Contribution to journalReview article

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