The albicidin resistance factor AlbD is a serine endopeptidase that hydrolyzes unusual oligoaromatic-type peptides

Vieweg Laura, Kretz Julian, Pesic Alexander, Kerwat Dennis, Grätz Stefan, Royer Monique, Cociancich Stéphane, Mainz Andi, Süssmuth Roderich. 2015. The albicidin resistance factor AlbD is a serine endopeptidase that hydrolyzes unusual oligoaromatic-type peptides. Journal of the American Chemical Society, 137 (4) : pp. 7608-7611.

Journal article ; Article de recherche ; Article de revue à facteur d'impact
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Abstract : The para-aminobenzoic acid-containing peptide albicidin is a pathogenicity factor synthesized by Xanthomonas albilineans in infections of sugar cane. Albicidin is a nanomolar inhibitor of the bacterial DNA gyrase with a strong activity against various Gram-negative bacteria. The bacterium Pantoea dispersa expresses the hydrolase AlbD, conferring natural resistance against albicidin. We show that AlbD is a novel type of endopeptidase that catalyzes the cleavage of albicidin at a peptide backbone amide bond, thus abolishing its antimicrobial activity. Additionally, we determined the minimal cleavage motif of AlbD with substrates derived by chemical synthesis. Our results clearly identify AlbD as a unique endopeptidase that is the first member of a new subfamily of peptidases. Our findings provide the molecular basis for a natural detoxification mechanism, potentially rendering a new tool in biological chemistry approaches. (Résumé d'auteur)

Mots-clés Agrovoc : Xanthomonas albilineans, Isomérase, Peptide, Composé aromatique, Antimicrobien, Acide benzoïque, Peptidase, Inhibiteur d'enzyme, Propriété antimicrobienne, Bactérie gram négatif, Détoxification métabolique, Activité enzymatique, Saccharum officinarum, Biologie moléculaire

Mots-clés complémentaires : Albicidine, Pantoea dispersa

Classification Agris : 000 - Other themes
H20 - Plant diseases

Champ stratégique Cirad : Axe 4 (2014-2018) - Santé des animaux et des plantes

Auteurs et affiliations

  • Vieweg Laura, Technische Universitaet Berlin (DEU)
  • Kretz Julian, Technische Universitaet Berlin (DEU)
  • Pesic Alexander, Technische Universitaet Berlin (DEU)
  • Kerwat Dennis, Technische Universitaet Berlin (DEU)
  • Grätz Stefan, Technische Universitaet Berlin (DEU)
  • Royer Monique, CIRAD-BIOS-UMR BGPI (FRA)
  • Cociancich Stéphane, CIRAD-BIOS-UMR BGPI (FRA)
  • Mainz Andi, Technische Universitaet Berlin (DEU)
  • Süssmuth Roderich, Technische Universitaet Berlin (DEU)

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