The albicidin resistance factor AlbD is a serine endopeptidase that hydrolyzes unusual oligoaromatic-type peptides
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.
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dig-cirad-fr-5779832024-01-28T23:00:53Z http://agritrop.cirad.fr/577983/ http://agritrop.cirad.fr/577983/ 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. Journal of the American Chemical Society, 137 (4) : 7608-7611.https://doi.org/10.1021/jacs.5b04099 <https://doi.org/10.1021/jacs.5b04099> 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 eng 2015 Journal of the American Chemical Society 000 - Autres thèmes H20 - Maladies des plantes 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 http://aims.fao.org/aos/agrovoc/c_27422 http://aims.fao.org/aos/agrovoc/c_3967 http://aims.fao.org/aos/agrovoc/c_5691 http://aims.fao.org/aos/agrovoc/c_622 http://aims.fao.org/aos/agrovoc/c_509 http://aims.fao.org/aos/agrovoc/c_881 http://aims.fao.org/aos/agrovoc/c_5690 http://aims.fao.org/aos/agrovoc/c_2599 http://aims.fao.org/aos/agrovoc/c_26756 http://aims.fao.org/aos/agrovoc/c_3352 http://aims.fao.org/aos/agrovoc/c_34050 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_6727 http://aims.fao.org/aos/agrovoc/c_4891 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. article info:eu-repo/semantics/article Journal Article info:eu-repo/semantics/publishedVersion http://agritrop.cirad.fr/577983/1/2015_JACS_Vieweg_AlbD.pdf text Cirad license info:eu-repo/semantics/restrictedAccess https://agritrop.cirad.fr/mention_legale.html https://doi.org/10.1021/jacs.5b04099 10.1021/jacs.5b04099 info:eu-repo/semantics/altIdentifier/doi/10.1021/jacs.5b04099 info:eu-repo/semantics/altIdentifier/purl/https://doi.org/10.1021/jacs.5b04099 |
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Biblioteca del CIRAD Francia |
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000 - Autres thèmes H20 - Maladies des plantes 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 http://aims.fao.org/aos/agrovoc/c_27422 http://aims.fao.org/aos/agrovoc/c_3967 http://aims.fao.org/aos/agrovoc/c_5691 http://aims.fao.org/aos/agrovoc/c_622 http://aims.fao.org/aos/agrovoc/c_509 http://aims.fao.org/aos/agrovoc/c_881 http://aims.fao.org/aos/agrovoc/c_5690 http://aims.fao.org/aos/agrovoc/c_2599 http://aims.fao.org/aos/agrovoc/c_26756 http://aims.fao.org/aos/agrovoc/c_3352 http://aims.fao.org/aos/agrovoc/c_34050 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_6727 http://aims.fao.org/aos/agrovoc/c_4891 000 - Autres thèmes H20 - Maladies des plantes 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 http://aims.fao.org/aos/agrovoc/c_27422 http://aims.fao.org/aos/agrovoc/c_3967 http://aims.fao.org/aos/agrovoc/c_5691 http://aims.fao.org/aos/agrovoc/c_622 http://aims.fao.org/aos/agrovoc/c_509 http://aims.fao.org/aos/agrovoc/c_881 http://aims.fao.org/aos/agrovoc/c_5690 http://aims.fao.org/aos/agrovoc/c_2599 http://aims.fao.org/aos/agrovoc/c_26756 http://aims.fao.org/aos/agrovoc/c_3352 http://aims.fao.org/aos/agrovoc/c_34050 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_6727 http://aims.fao.org/aos/agrovoc/c_4891 |
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000 - Autres thèmes H20 - Maladies des plantes 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 http://aims.fao.org/aos/agrovoc/c_27422 http://aims.fao.org/aos/agrovoc/c_3967 http://aims.fao.org/aos/agrovoc/c_5691 http://aims.fao.org/aos/agrovoc/c_622 http://aims.fao.org/aos/agrovoc/c_509 http://aims.fao.org/aos/agrovoc/c_881 http://aims.fao.org/aos/agrovoc/c_5690 http://aims.fao.org/aos/agrovoc/c_2599 http://aims.fao.org/aos/agrovoc/c_26756 http://aims.fao.org/aos/agrovoc/c_3352 http://aims.fao.org/aos/agrovoc/c_34050 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_6727 http://aims.fao.org/aos/agrovoc/c_4891 000 - Autres thèmes H20 - Maladies des plantes 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 http://aims.fao.org/aos/agrovoc/c_27422 http://aims.fao.org/aos/agrovoc/c_3967 http://aims.fao.org/aos/agrovoc/c_5691 http://aims.fao.org/aos/agrovoc/c_622 http://aims.fao.org/aos/agrovoc/c_509 http://aims.fao.org/aos/agrovoc/c_881 http://aims.fao.org/aos/agrovoc/c_5690 http://aims.fao.org/aos/agrovoc/c_2599 http://aims.fao.org/aos/agrovoc/c_26756 http://aims.fao.org/aos/agrovoc/c_3352 http://aims.fao.org/aos/agrovoc/c_34050 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_6727 http://aims.fao.org/aos/agrovoc/c_4891 Vieweg, Laura Kretz, Julian Pesic, Alexander Kerwat, Dennis Grätz, Stefan Royer, Monique Cociancich, Stéphane Mainz, Andi Süssmuth, Roderich The albicidin resistance factor AlbD is a serine endopeptidase that hydrolyzes unusual oligoaromatic-type peptides |
description |
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. |
format |
article |
topic_facet |
000 - Autres thèmes H20 - Maladies des plantes 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 http://aims.fao.org/aos/agrovoc/c_27422 http://aims.fao.org/aos/agrovoc/c_3967 http://aims.fao.org/aos/agrovoc/c_5691 http://aims.fao.org/aos/agrovoc/c_622 http://aims.fao.org/aos/agrovoc/c_509 http://aims.fao.org/aos/agrovoc/c_881 http://aims.fao.org/aos/agrovoc/c_5690 http://aims.fao.org/aos/agrovoc/c_2599 http://aims.fao.org/aos/agrovoc/c_26756 http://aims.fao.org/aos/agrovoc/c_3352 http://aims.fao.org/aos/agrovoc/c_34050 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_6727 http://aims.fao.org/aos/agrovoc/c_4891 |
author |
Vieweg, Laura Kretz, Julian Pesic, Alexander Kerwat, Dennis Grätz, Stefan Royer, Monique Cociancich, Stéphane Mainz, Andi Süssmuth, Roderich |
author_facet |
Vieweg, Laura Kretz, Julian Pesic, Alexander Kerwat, Dennis Grätz, Stefan Royer, Monique Cociancich, Stéphane Mainz, Andi Süssmuth, Roderich |
author_sort |
Vieweg, Laura |
title |
The albicidin resistance factor AlbD is a serine endopeptidase that hydrolyzes unusual oligoaromatic-type peptides |
title_short |
The albicidin resistance factor AlbD is a serine endopeptidase that hydrolyzes unusual oligoaromatic-type peptides |
title_full |
The albicidin resistance factor AlbD is a serine endopeptidase that hydrolyzes unusual oligoaromatic-type peptides |
title_fullStr |
The albicidin resistance factor AlbD is a serine endopeptidase that hydrolyzes unusual oligoaromatic-type peptides |
title_full_unstemmed |
The albicidin resistance factor AlbD is a serine endopeptidase that hydrolyzes unusual oligoaromatic-type peptides |
title_sort |
albicidin resistance factor albd is a serine endopeptidase that hydrolyzes unusual oligoaromatic-type peptides |
url |
http://agritrop.cirad.fr/577983/ http://agritrop.cirad.fr/577983/1/2015_JACS_Vieweg_AlbD.pdf |
work_keys_str_mv |
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