title: Characterization of amylolysin, a novel lantibiotic from Bacillus amyloliquefaciens GA1.
abstract: BACKGROUND
  Lantibiotics are heat-stable peptides characterized by the presence of thioether amino acid lanthionine and methyllanthionine. They are capable to inhibit the growth of Gram-positive bacteria, including Listeria monocytogenes, Staphylococcus aureus or Bacillus cereus, the causative agents of food-borne diseases or nosocomial infections. Lantibiotic biosynthetic machinery is encoded by gene cluster composed by a structural gene that codes for a pre-lantibiotic peptide and other genes involved in pre-lantibiotic modifications, regulation, export and immunity.
  
  
  RESULTS
  Bacillus amyloliquefaciens GA1 was found to produce an antimicrobial peptide, named amylolysin, active on an array of Gram-positive bacteria, including methicillin resistant S. aureus. Genome characterization led to the identification of a putative lantibiotic gene cluster that comprises a structural gene (amlA) and genes involved in modification (amlM), transport (amlT), regulation (amlKR) and immunity (amlFE). Disruption of amlA led to loss of biological activity, confirming thus that the identified gene cluster is related to amylolysin synthesis. MALDI-TOF and LC-MS analysis on purified amylolysin demonstrated that this latter corresponds to a novel lantibiotic not described to date. The ability of amylolysin to interact in vitro with the lipid II, the carrier of peptidoglycan monomers across the cytoplasmic membrane and the presence of a unique modification gene suggest that the identified peptide belongs to the group B lantibiotic. Amylolysin immunity seems to be driven by only two AmlF and AmlE proteins, which is uncommon within the Bacillus genus.
  
  
  CONCLUSIONS
  Apart from mersacidin produced by Bacillus amyloliquefaciens strains Y2 and HIL Y-85,544728, reports on the synthesis of type B-lantibiotic in this species are scarce. This study reports on a genetic and structural characterization of another representative of the type B lantibiotic in B. amyloliquefaciens.
authors.affiliation: Centre d'Ingénierie des Protéines, Bacterial Physiology and Genetics, Université de Liège, Liège, Belgium.
authors.forename: Anthony
authors.initials: A
authors.lastname: Arguelles Arias
authors.affiliation: Centre Wallon de Biologie Industrielle, Unité de Bioindustrie, Faculté de Sciences Agronomique de Gembloux, Gembloux, Belgium .
authors.forename: Marc
authors.initials: M
authors.lastname: Ongena
authors.affiliation: Laboratorium voor Eiwitbiochemie en Eiwitengineering, Universiteit-Gent, Gent, Belgium.
authors.forename: Bart
authors.initials: B
authors.lastname: Devreese
authors.affiliation: Centre d'Ingénierie des Protéines, Bacterial Physiology and Genetics, Université de Liège, Liège, Belgium.
authors.forename: Mohammed
authors.initials: M
authors.lastname: Terrak
authors.affiliation: Centre d'Ingénierie des Protéines, Bacterial Physiology and Genetics, Université de Liège, Liège, Belgium.
authors.forename: Bernard
authors.initials: B
authors.lastname: Joris
authors.affiliation: Unité de Biotechnologies et Bioprocédés, Université Libre de Bruxelles, Brussels, Belgium.
authors.forename: Patrick
authors.initials: P
authors.lastname: Fickers
mesh_terms: D001407:Bacillus / Q000235:genetics* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D001430:Bacteriocins / Q000096:biosynthesis* / Q000235:genetics* / Q000302:isolation & purification / Q000494:pharmacology; D005798:Genes, Bacterial; D006094:Gram-Positive Bacteria / Q000254:growth & development; D014538:Uridine Diphosphate N-Acetylmuramic Acid / Q000031:analogs & derivatives / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D001430:Bacteriocins; D014538:Uridine Diphosphate N-Acetylmuramic Acid; C000592191:amylolysin, Bacillus amyloliquefaciens GA1; C069249:muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol