On Blastocystis secreted cysteine proteases: ...
Type de document :
Compte-rendu et recension critique d'ouvrage
PMID :
Titre :
On Blastocystis secreted cysteine proteases: a legumain-activated cathepsin B increases paracellular permeability of intestinal Caco-2 cell monolayers
Auteur(s) :
Nourrisson, C. [Auteur]
Laboratoire Microorganismes : Génome et Environnement [LMGE]
Université Blaise Pascal - Clermont-Ferrand 2 [UBP]
Wawrzyniak, I. [Auteur]
Laboratoire Microorganismes : Génome et Environnement [LMGE]
Université Clermont Auvergne [2017-2020] [UCA [2017-2020]]
Cian, A. [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Institut Pasteur de Lille
Université Lille Nord de France (COMUE)
Livrelli, Valerie [Auteur]
Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte [M2iSH]
Viscogliosi, F. [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Centre National de la Recherche Scientifique [CNRS]
Institut Pasteur de Lille
Université Lille Nord de France (COMUE)
Delbac, F. [Auteur]
Laboratoire Microorganismes : Génome et Environnement [LMGE]
Université Clermont Auvergne [2017-2020] [UCA [2017-2020]]
Poirier, P. [Auteur]
Laboratoire Microorganismes : Génome et Environnement [LMGE]
Laboratoire Microorganismes : Génome et Environnement [LMGE]
Université Blaise Pascal - Clermont-Ferrand 2 [UBP]
Wawrzyniak, I. [Auteur]
Laboratoire Microorganismes : Génome et Environnement [LMGE]
Université Clermont Auvergne [2017-2020] [UCA [2017-2020]]
Cian, A. [Auteur]
Centre National de la Recherche Scientifique [CNRS]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Institut Pasteur de Lille
Université Lille Nord de France (COMUE)
Livrelli, Valerie [Auteur]
Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte [M2iSH]
Viscogliosi, F. [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Centre National de la Recherche Scientifique [CNRS]
Institut Pasteur de Lille
Université Lille Nord de France (COMUE)
Delbac, F. [Auteur]
Laboratoire Microorganismes : Génome et Environnement [LMGE]
Université Clermont Auvergne [2017-2020] [UCA [2017-2020]]
Poirier, P. [Auteur]
Laboratoire Microorganismes : Génome et Environnement [LMGE]
Titre de la revue :
Parasitology
Pagination :
1713-1722
Éditeur :
Cambridge University Press
Date de publication :
2016
ISSN :
0031-1820
Mot(s)-clé(s) en anglais :
Caco-2
permeability
Blastocystis
cysteine proteases
Cathepsin B
Legumain
permeability
Blastocystis
cysteine proteases
Cathepsin B
Legumain
Discipline(s) HAL :
Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Protistologie
Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Bactériologie
Sciences du Vivant [q-bio]/Médecine humaine et pathologie/Maladies infectieuses
Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Bactériologie
Sciences du Vivant [q-bio]/Médecine humaine et pathologie/Maladies infectieuses
Résumé en anglais : [en]
Blastocystis spp. pathogenic potential remains unclear as these anaerobic parasitic protozoa are frequently isolated from stools of both symptomatic and asymptomatic subjects. In silico analysis of the whole genome sequence ...
Lire la suite >Blastocystis spp. pathogenic potential remains unclear as these anaerobic parasitic protozoa are frequently isolated from stools of both symptomatic and asymptomatic subjects. In silico analysis of the whole genome sequence of Blastocystis subtype 7 revealed the presence of numerous proteolytic enzymes including cysteine proteases predicted to be secreted. To assess the potential impact of proteases on intestinal cells and gut function, we focused our study on two cysteine proteases, a legumain and a cathepsin B, which were previously identified in Blastocystis subtype 7 culture supernatants. Both cysteine proteases were produced as active recombinant proteins. Activation of the recombinant legumain was shown to be autocatalytic and triggered by acidic pH, whereas proteolytic activity of the recombinant cathepsin B was only recorded after co-incubation with the legumain. We then measured the diffusion of 4-kDa FITC-labelled dextran across Caco-2 cell monolayers following exposition to either Blastocystis culture supernatants or each recombinant protease. Both Blastocystis culture supernatants and recombinant activated cathepsin B induced an increase of Caco-2 cell monolayer permeability, and this effect was significantly inhibited by E-64, a specific cysteine protease inhibitor. Our results suggest that cathepsin B might play a role in pathogenesis of Blastocystis by increasing intestinal cell permeability.Lire moins >
Lire la suite >Blastocystis spp. pathogenic potential remains unclear as these anaerobic parasitic protozoa are frequently isolated from stools of both symptomatic and asymptomatic subjects. In silico analysis of the whole genome sequence of Blastocystis subtype 7 revealed the presence of numerous proteolytic enzymes including cysteine proteases predicted to be secreted. To assess the potential impact of proteases on intestinal cells and gut function, we focused our study on two cysteine proteases, a legumain and a cathepsin B, which were previously identified in Blastocystis subtype 7 culture supernatants. Both cysteine proteases were produced as active recombinant proteins. Activation of the recombinant legumain was shown to be autocatalytic and triggered by acidic pH, whereas proteolytic activity of the recombinant cathepsin B was only recorded after co-incubation with the legumain. We then measured the diffusion of 4-kDa FITC-labelled dextran across Caco-2 cell monolayers following exposition to either Blastocystis culture supernatants or each recombinant protease. Both Blastocystis culture supernatants and recombinant activated cathepsin B induced an increase of Caco-2 cell monolayer permeability, and this effect was significantly inhibited by E-64, a specific cysteine protease inhibitor. Our results suggest that cathepsin B might play a role in pathogenesis of Blastocystis by increasing intestinal cell permeability.Lire moins >
Langue :
Anglais
Vulgarisation :
Non
Source :