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) : 7608-7611.

https://doi.org/10.1021/jacs.5b04099

Article de revue ; Article de recherche ; Article de revue à facteur d'impact

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Quartile : Outlier, Sujet : CHEMISTRY, MULTIDISCIPLINARY

Résumé : 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.

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