Exposure to a cutinase-like serine esterase ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
Exposure to a cutinase-like serine esterase triggers rapid lysis of multiple mycobacterial species
Auteur(s) :
Yang, Yong [Auteur]
Bhatti, Alexandra [Auteur]
Ke, Danxia [Auteur]
Gonzalez-Juarrero, Mercedes [Auteur]
Lenaerts, Anne [Auteur]
Kremer, Laurent [Auteur]
Guerardel, Yann [Auteur]
Zhang, Peijun [Auteur]
Ojha, Anil K. [Auteur]
Bhatti, Alexandra [Auteur]
Ke, Danxia [Auteur]
Gonzalez-Juarrero, Mercedes [Auteur]
Lenaerts, Anne [Auteur]
Kremer, Laurent [Auteur]
Guerardel, Yann [Auteur]
Zhang, Peijun [Auteur]
Ojha, Anil K. [Auteur]
Titre de la revue :
The Journal of biological chemistry
Nom court de la revue :
J. Biol. Chem.
Numéro :
288
Pagination :
382-392
Date de publication :
2013-01-04
ISSN :
1083-351X
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
Mycobacteria are shaped by a thick envelope made of an array of uniquely structured lipids and polysaccharides. However, the spatial organization of these molecules remains unclear. Here, we show that exposure to an esterase ...
Lire la suite >Mycobacteria are shaped by a thick envelope made of an array of uniquely structured lipids and polysaccharides. However, the spatial organization of these molecules remains unclear. Here, we show that exposure to an esterase from Mycobacterium smegmatis (Msmeg_1529), hydrolyzing the ester linkage of trehalose dimycolate in vitro, triggers rapid and efficient lysis of Mycobacterium tuberculosis, Mycobacterium bovis BCG, and Mycobacterium marinum. Exposure to the esterase immediately releases free mycolic acids, while concomitantly depleting trehalose mycolates. Moreover, lysis could be competitively inhibited by an excess of purified trehalose dimycolate and was abolished by a S124A mutation affecting the catalytic activity of the esterase. These findings are consistent with an indispensable structural role of trehalose mycolates in the architectural design of the exposed surface of the mycobacterial envelope. Importantly, we also demonstrate that the esterase-mediated rapid lysis of M. tuberculosis significantly improves its detection in paucibacillary samples.Lire moins >
Lire la suite >Mycobacteria are shaped by a thick envelope made of an array of uniquely structured lipids and polysaccharides. However, the spatial organization of these molecules remains unclear. Here, we show that exposure to an esterase from Mycobacterium smegmatis (Msmeg_1529), hydrolyzing the ester linkage of trehalose dimycolate in vitro, triggers rapid and efficient lysis of Mycobacterium tuberculosis, Mycobacterium bovis BCG, and Mycobacterium marinum. Exposure to the esterase immediately releases free mycolic acids, while concomitantly depleting trehalose mycolates. Moreover, lysis could be competitively inhibited by an excess of purified trehalose dimycolate and was abolished by a S124A mutation affecting the catalytic activity of the esterase. These findings are consistent with an indispensable structural role of trehalose mycolates in the architectural design of the exposed surface of the mycobacterial envelope. Importantly, we also demonstrate that the esterase-mediated rapid lysis of M. tuberculosis significantly improves its detection in paucibacillary samples.Lire moins >
Langue :
Anglais
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Glycobiologie structurale des interactions hôtes-pathogènes
Date de dépôt :
2020-02-12T15:11:09Z