Domains of BclA, the major surface ...
Type de document :
Article dans une revue scientifique
URL permanente :
Titre :
Domains of BclA, the major surface glycoprotein of the B. cereus exosporium: glycosylation patterns and role in spore surface properties
Auteur(s) :
Lequette, Yannick [Auteur]
Processus aux Interfaces et Hygiène des Matériaux [PIHM]
Garénaux, Estelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Combrouse, Typhaine [Auteur]
Processus aux Interfaces et Hygiène des Matériaux [PIHM]
Lima Dias, Thays Del [Auteur]
Processus aux Interfaces et Hygiène des Matériaux [PIHM]
Ronse, Annette [Auteur]
Processus aux Interfaces et Hygiène des Matériaux [PIHM]
Slomianny, Christian [Auteur]
Laboratoire de Physiologie Cellulaire - U 1003 [PHYCELL]
Trivelli, Xavier [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Faille, Christine [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Processus aux Interfaces et Hygiène des Matériaux [PIHM]
Garénaux, Estelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Combrouse, Typhaine [Auteur]
Processus aux Interfaces et Hygiène des Matériaux [PIHM]
Lima Dias, Thays Del [Auteur]
Processus aux Interfaces et Hygiène des Matériaux [PIHM]
Ronse, Annette [Auteur]
Processus aux Interfaces et Hygiène des Matériaux [PIHM]
Slomianny, Christian [Auteur]
Laboratoire de Physiologie Cellulaire - U 1003 [PHYCELL]
Trivelli, Xavier [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Faille, Christine [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Titre de la revue :
Biofouling
Numéro :
27
Pagination :
751-761
Date de publication :
2011
Mot(s)-clé(s) en anglais :
Bacillus spore
exosporium
BclA domains
carbohydrates
adhesion
physicochemistry
exosporium
BclA domains
carbohydrates
adhesion
physicochemistry
Discipline(s) HAL :
Sciences du Vivant [q-bio]/Ingénierie des aliments
Physique [physics]/Matière Condensée [cond-mat]/Science des matériaux [cond-mat.mtrl-sci]
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
Physique [physics]/Matière Condensée [cond-mat]/Matière Molle [cond-mat.soft]
Sciences de l'ingénieur [physics]/Génie des procédés
Physique [physics]/Matière Condensée [cond-mat]/Science des matériaux [cond-mat.mtrl-sci]
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
Physique [physics]/Matière Condensée [cond-mat]/Matière Molle [cond-mat.soft]
Sciences de l'ingénieur [physics]/Génie des procédés
Résumé en anglais : [en]
The role of the BclA domains of B. cereus ATCC 14579 was investigated in order to understand the phenomena involved in the interfacial processes occurring between spores and inert surfaces. This was done by (i) creating ...
Lire la suite >The role of the BclA domains of B. cereus ATCC 14579 was investigated in order to understand the phenomena involved in the interfacial processes occurring between spores and inert surfaces. This was done by (i) creating deletions in the collagen-like region (CLR) and the C-terminal domain (CTD) of BclA, (ii) building BclA proteins with various lengths in the CLR and (iii) modifying the hydrophobic upper surface in the CTD. First, it was demonstrated that the CLR was substituted by three residues already reported in the CLR of B. anthracis, viz. rhamnose, 3-O-methyl-rhamnose, and GalNH2 residues, while the CTD was also substituted by two additional glycosyl residues, viz. 2-O-methyl-rhamnose and 2,4-O-methyl-rhamnose. Regarding the properties of the spores, both CLR and CTD contributed to the adhesion of the spores, which was estimated by measuring the resistance to detachment of spores adhered to stainless steel plates). CLR and CTD also impacted the hydrophobic character and isoelectric point of the spores. It was then shown that the resistance to detachment of the spores was not affected by the physicochemical properties, but by the CLR length and the presence of hydrophobic amino acids on the CTD.Lire moins >
Lire la suite >The role of the BclA domains of B. cereus ATCC 14579 was investigated in order to understand the phenomena involved in the interfacial processes occurring between spores and inert surfaces. This was done by (i) creating deletions in the collagen-like region (CLR) and the C-terminal domain (CTD) of BclA, (ii) building BclA proteins with various lengths in the CLR and (iii) modifying the hydrophobic upper surface in the CTD. First, it was demonstrated that the CLR was substituted by three residues already reported in the CLR of B. anthracis, viz. rhamnose, 3-O-methyl-rhamnose, and GalNH2 residues, while the CTD was also substituted by two additional glycosyl residues, viz. 2-O-methyl-rhamnose and 2,4-O-methyl-rhamnose. Regarding the properties of the spores, both CLR and CTD contributed to the adhesion of the spores, which was estimated by measuring the resistance to detachment of spores adhered to stainless steel plates). CLR and CTD also impacted the hydrophobic character and isoelectric point of the spores. It was then shown that the resistance to detachment of the spores was not affected by the physicochemical properties, but by the CLR length and the presence of hydrophobic amino acids on the CTD.Lire moins >
Langue :
Anglais
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
Université de Lille
Inserm
CNRS
Inserm
CNRS
Collections :
Équipe(s) de recherche :
Processus aux Interfaces et Hygiène des Matériaux (PIHM)
Date de dépôt :
2019-05-16T16:44:40Z
2021-03-19T08:24:47Z
2021-05-17T13:33:59Z
2021-03-19T08:24:47Z
2021-05-17T13:33:59Z