Differentiation of Crohn’s Disease-Associated ...
Document type :
Compte-rendu et recension critique d'ouvrage
DOI :
Title :
Differentiation of Crohn’s Disease-Associated Isolates from Other Pathogenic Escherichia coli by Fimbrial Adhesion under Shear Force
Author(s) :
Szunerits, Sabine [Auteur]
Institut d’Électronique, de Microélectronique et de Nanotechnologie - UMR 8520 [IEMN]
Zagorodko, Oleksandr [Auteur]
Cogez, Virginie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Dumych, Tetiana [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Chalopin, Thibaut [Auteur]
Chimie Et Interdisciplinarité : Synthèse, Analyse, Modélisation [CEISAM]
Alvarez Dorta, Dimitri [Auteur]
Sivignon, Adeline [Auteur]
Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte [M2iSH]
Barnich, Nicolas [Auteur]
Département Microbiologie et Chaîne Alimentaire [MICA]
Harduin-Lepers, Anne [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Larroulet, Iban [Auteur]
Yanguas Serrano, Aritz [Auteur]
Siriwardena, Aloysius [Auteur]
Laboratoire de Glycochimie, des Antimicrobiens et des Agro-ressources - UMR CNRS 7378 [LG2A ]
Pesquera, Amaia [Auteur]
Zurutuza, Amaia [Auteur]
Gouin, Sébastien [Auteur]
Chimie Et Interdisciplinarité : Synthèse, Analyse, Modélisation [CEISAM]
Boukherroub, Rabah [Auteur]
Institut d’Électronique, de Microélectronique et de Nanotechnologie - UMR 8520 [IEMN]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Bouckaert, Julie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]

Institut d’Électronique, de Microélectronique et de Nanotechnologie - UMR 8520 [IEMN]
Zagorodko, Oleksandr [Auteur]
Cogez, Virginie [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Dumych, Tetiana [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Chalopin, Thibaut [Auteur]
Chimie Et Interdisciplinarité : Synthèse, Analyse, Modélisation [CEISAM]
Alvarez Dorta, Dimitri [Auteur]
Sivignon, Adeline [Auteur]
Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte [M2iSH]
Barnich, Nicolas [Auteur]
Département Microbiologie et Chaîne Alimentaire [MICA]
Harduin-Lepers, Anne [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Larroulet, Iban [Auteur]
Yanguas Serrano, Aritz [Auteur]
Siriwardena, Aloysius [Auteur]
Laboratoire de Glycochimie, des Antimicrobiens et des Agro-ressources - UMR CNRS 7378 [LG2A ]
Pesquera, Amaia [Auteur]
Zurutuza, Amaia [Auteur]
Gouin, Sébastien [Auteur]
Chimie Et Interdisciplinarité : Synthèse, Analyse, Modélisation [CEISAM]
Boukherroub, Rabah [Auteur]

Institut d’Électronique, de Microélectronique et de Nanotechnologie - UMR 8520 [IEMN]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Bouckaert, Julie [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Journal title :
Biology
Publisher :
MDPI
Publication date :
2016-06
ISSN :
2079-7737
English keyword(s) :
adherent-invasive Escherichia coli
shear force
surface plasmon resonance
graphene
heptyl α-D-mannose
shear force
surface plasmon resonance
graphene
heptyl α-D-mannose
HAL domain(s) :
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
English abstract : [en]
Shear force exerted on uropathogenic Escherichia coli adhering to surfaces makes type-1 fimbriae stretch out like springs to catch on to mannosidic receptors. This mechanism is initiated by a disruption of the quaternary ...
Show more >Shear force exerted on uropathogenic Escherichia coli adhering to surfaces makes type-1 fimbriae stretch out like springs to catch on to mannosidic receptors. This mechanism is initiated by a disruption of the quaternary interactions between the lectin and the pilin of the two-domain FimH adhesin and transduces allosterically to the mannose-binding pocket of FimH to increase its affinity. Mannose-specific adhesion of 14 E. coli pathovars was measured under flow, using surface plasmon resonance detection on functionalized graphene-coated gold interfaces. Increasing the shear had important differential consequences on bacterial adhesion. Adherent-invasive E. coli, isolated from the feces and biopsies of Crohn's disease patients, consistently changed their adhesion behavior less under shear and displayed lower SPR signals, compared to E. coli opportunistically infecting the urinary tract, intestines or loci of knee and hip prostheses. We exemplified this further with the extreme behaviors of the reference strains UTI89 and LF82. Whereas their FimA major pilins have identical sequences, FimH of LF82 E. coli is marked by the Thr158Pro mutation. Positioned in the inter-domain region known to carry hot spots of mutations in E. coli pathotypes, residue 158 is indicated to play a structural role in the allosteric regulation of type-1 fimbriae-mediated bacterial adhesion.Show less >
Show more >Shear force exerted on uropathogenic Escherichia coli adhering to surfaces makes type-1 fimbriae stretch out like springs to catch on to mannosidic receptors. This mechanism is initiated by a disruption of the quaternary interactions between the lectin and the pilin of the two-domain FimH adhesin and transduces allosterically to the mannose-binding pocket of FimH to increase its affinity. Mannose-specific adhesion of 14 E. coli pathovars was measured under flow, using surface plasmon resonance detection on functionalized graphene-coated gold interfaces. Increasing the shear had important differential consequences on bacterial adhesion. Adherent-invasive E. coli, isolated from the feces and biopsies of Crohn's disease patients, consistently changed their adhesion behavior less under shear and displayed lower SPR signals, compared to E. coli opportunistically infecting the urinary tract, intestines or loci of knee and hip prostheses. We exemplified this further with the extreme behaviors of the reference strains UTI89 and LF82. Whereas their FimA major pilins have identical sequences, FimH of LF82 E. coli is marked by the Thr158Pro mutation. Positioned in the inter-domain region known to carry hot spots of mutations in E. coli pathotypes, residue 158 is indicated to play a structural role in the allosteric regulation of type-1 fimbriae-mediated bacterial adhesion.Show less >
Language :
Anglais
Popular science :
Non
Source :
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