Publications des agents du Cirad


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

Vieweg L., Kretz J., Pesic A., Kerwat D., Grätz S., Royer M., Cociancich S., Mainz A., Süssmuth R.. 2015. Journal of the American Chemical Society, 137 (4) : p. 7608-7611.

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 : biologie moléculaire; saccharum officinarum; activité enzymatique; détoxification métabolique; bactérie gram négatif; propriété antimicrobienne; inhibiteur d'enzyme; peptidase; acide benzoïque; antimicrobien; composé aromatique; peptide; isomérase; xanthomonas albilineans; pantoea dispersa; albicidine

Thématique : Autres thèmes; Maladies des plantes

Documents associés

Article de revue

Agents Cirad, auteurs de cette publication :