Unraveling the role of surface mucus-binding ...
Document type :
Article dans une revue scientifique
PMID :
Permalink :
Title :
Unraveling the role of surface mucus-binding protein and pili in muco-adhesion of Lactococcus lactis
Author(s) :
Le, Doan Thanh Lam [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Tran, Thi-Ly [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Duviau, Marie-Pierre [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Meyrand, Mickael [Auteur]
Institut National de la Recherche Agronomique [INRA]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Castelain, Mickaël [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Loubière, Pascal [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Chapot-Chartier, Marie-Pierre [Auteur]
Institut National de la Recherche Agronomique [INRA]
Dague, Etienne [Auteur]
Laboratoire d'analyse et d'architecture des systèmes [LAAS]
Mercier-Bonin, Muriel [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Tran, Thi-Ly [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Duviau, Marie-Pierre [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Meyrand, Mickael [Auteur]
Institut National de la Recherche Agronomique [INRA]
Guerardel, Yann [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Castelain, Mickaël [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Loubière, Pascal [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Chapot-Chartier, Marie-Pierre [Auteur]
Institut National de la Recherche Agronomique [INRA]
Dague, Etienne [Auteur]
Laboratoire d'analyse et d'architecture des systèmes [LAAS]
Mercier-Bonin, Muriel [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Journal title :
PLoS One
Abbreviated title :
PLoS ONE
Volume number :
8
Publication date :
2013
ISSN :
1932-6203
English keyword(s) :
Lactococcus lactis
adhesives
Pili and fimbriae
shear stresses
polystyrene
coatings
mucin
bacteria
adhesives
Pili and fimbriae
shear stresses
polystyrene
coatings
mucin
bacteria
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
Adhesion of bacteria to mucus may favor their persistence within the gut and their beneficial effects to the host. Interactions between pig gastric mucin (PGM) and a natural isolate of Lactococcus lactis (TIL448) were ...
Show more >Adhesion of bacteria to mucus may favor their persistence within the gut and their beneficial effects to the host. Interactions between pig gastric mucin (PGM) and a natural isolate of Lactococcus lactis (TIL448) were measured at the single-cell scale and under static conditions, using atomic force microscopy (AFM). In parallel, these interactions were monitored at the bacterial population level and under shear flow. AFM experiments with a L. lactis cell-probe and a PGM-coated surface revealed a high proportion of specific adhesive events (60%) and a low level of non-adhesive ones (2%). The strain muco-adhesive properties were confirmed by the weak detachment of bacteria from the PGM-coated surface under shear flow. In AFM, rupture events were detected at short (100-200 nm) and long distances (up to 600-800 nm). AFM measurements on pili and mucus-binding protein defective mutants demonstrated the comparable role played by these two surface proteinaceous components in adhesion to PGM under static conditions. Under shear flow, a more important contribution of the mucus-binding protein than the pili one was observed. Both methods differ by the way of probing the adhesion force, i.e. negative force contact vs. sedimentation and normal-to-substratum retraction vs. tangential detachment conditions, using AFM and flow chamber, respectively. AFM blocking assays with free PGM or O-glycan fractions purified from PGM demonstrated that neutral oligosaccharides played a major role in adhesion of L. lactis TIL448 to PGM. This study dissects L. lactis muco-adhesive phenotype, in relation with the nature of the bacterial surface determinants.Show less >
Show more >Adhesion of bacteria to mucus may favor their persistence within the gut and their beneficial effects to the host. Interactions between pig gastric mucin (PGM) and a natural isolate of Lactococcus lactis (TIL448) were measured at the single-cell scale and under static conditions, using atomic force microscopy (AFM). In parallel, these interactions were monitored at the bacterial population level and under shear flow. AFM experiments with a L. lactis cell-probe and a PGM-coated surface revealed a high proportion of specific adhesive events (60%) and a low level of non-adhesive ones (2%). The strain muco-adhesive properties were confirmed by the weak detachment of bacteria from the PGM-coated surface under shear flow. In AFM, rupture events were detected at short (100-200 nm) and long distances (up to 600-800 nm). AFM measurements on pili and mucus-binding protein defective mutants demonstrated the comparable role played by these two surface proteinaceous components in adhesion to PGM under static conditions. Under shear flow, a more important contribution of the mucus-binding protein than the pili one was observed. Both methods differ by the way of probing the adhesion force, i.e. negative force contact vs. sedimentation and normal-to-substratum retraction vs. tangential detachment conditions, using AFM and flow chamber, respectively. AFM blocking assays with free PGM or O-glycan fractions purified from PGM demonstrated that neutral oligosaccharides played a major role in adhesion of L. lactis TIL448 to PGM. This study dissects L. lactis muco-adhesive phenotype, in relation with the nature of the bacterial surface determinants.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
Chemical Glycobiology
Submission date :
2020-02-12T15:11:08Z
2021-02-26T14:25:59Z
2021-02-26T14:25:59Z
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