Titre :

Exposure to a cutinase-like serine esterase triggers rapid lysis of multiple mycobacterial species

Auteur(s) :

Yang, Yong [Auteur]
University of Pittsburgh [PITT]
Bhatti, Alexandra [Auteur]
University of Pittsburgh [PITT]
Ke, Danxia [Auteur]
University of Pittsburgh [PITT]
Gonzalez-Juarrero, Mercedes [Auteur]
Colorado State University [Fort Collins] [CSU]
Lenaerts, Anne [Auteur]
Colorado State University [Fort Collins] [CSU]
Kremer, Laurent [Auteur]
Dynamique des interactions membranaires normales et pathologiques [DIMNP]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Zhang, Peijun [Auteur]
University of Pittsburgh [PITT]
Ojha, Anil K. [Auteur]
University of Pittsburgh [PITT]

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

Mot(s)-clé(s) en anglais :

Carboxylesterase
Glycolipids
Lipids
Membrane Bilayer
Mycobacteria
Lysis
Mycobacteria-
Outer Membrane
Serine Esterase
Trehalose Mycolates

Discipline(s) HAL :

Chimie/Chimie théorique et/ou physique
Sciences du Vivant [q-bio]

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 >

Langue :

Anglais

Audience :

Non spécifiée

Établissement(s) :

CNRS
Université de Lille

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Équipe(s) de recherche :

Chemical Glycobiology

Date de dépôt :

2020-02-12T15:11:09Z
2021-03-03T08:53:54Z