New developments in lantibiotic biosynthesis and mode of action

Gregory C. Patton, Wilfred A. Van Der Donk

Research output: Contribution to journalReview article

Abstract

Lantibiotics are a unique class of peptide antibiotics. Recent studies of the proteins involved in the elaborate post-translational modifications of lantibiotics have revealed that these enzymes have relaxed substrate specificity. These modifications include the dehydration of serine and threonine residues followed by the intramolecular addition of cysteine thiols to the unsaturated amino acids to create an intricate polycyclic peptide. The use of peptide engineering in vivo and in vitro has allowed investigation of their biosynthetic machinery. Several members utilize a unique mode of biological action that involves the sequestration of lipid II, a crucial intermediate in peptidoglycan biosynthesis, to form pores in bacterial membranes.

Original languageEnglish (US)
Pages (from-to)543-551
Number of pages9
JournalCurrent Opinion in Microbiology
Volume8
Issue number5
DOIs
StatePublished - Oct 1 2005

Fingerprint

Bacteriocins
Peptides
Peptidoglycan
Threonine
Post Translational Protein Processing
Substrate Specificity
Dehydration
Sulfhydryl Compounds
Serine
Cysteine
Anti-Bacterial Agents
Amino Acids
Membranes
Enzymes
Proteins

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)
  • Infectious Diseases

Cite this

New developments in lantibiotic biosynthesis and mode of action. / Patton, Gregory C.; Van Der Donk, Wilfred A.

In: Current Opinion in Microbiology, Vol. 8, No. 5, 01.10.2005, p. 543-551.

Research output: Contribution to journalReview article

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