Receptor recognition by meningococcal type ...
Document type :
Article dans une revue scientifique
DOI :
Permalink :
Title :
Receptor recognition by meningococcal type IV pili relies on a specific complex N-glycan
Author(s) :
Le Guennec, Loic [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Virion, Zoé [Auteur]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
Université Paris Descartes - Paris 5 [UPD5]
Bouzinba-Ségard, Haniaa [Auteur]
Université Paris Descartes - Paris 5 [UPD5]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Masselot, Catherine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Leonard, Renaud [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Nassif, Xavier [Auteur]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
CHU Necker - Enfants Malades [AP-HP]
Université Paris Descartes - Paris 5 [UPD5]
Bourdoulous, Sandrine [Auteur]
Université Paris Descartes - Paris 5 [UPD5]
Institut Cochin [UMR_S567 / UMR 8104]
Coureuil, Mathieu [Auteur]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
CHU Necker - Enfants Malades [AP-HP]
Université Paris Descartes - Paris 5 [UPD5]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Virion, Zoé [Auteur]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
Université Paris Descartes - Paris 5 [UPD5]
Bouzinba-Ségard, Haniaa [Auteur]
Université Paris Descartes - Paris 5 [UPD5]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Masselot, Catherine [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Leonard, Renaud [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Nassif, Xavier [Auteur]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
CHU Necker - Enfants Malades [AP-HP]
Université Paris Descartes - Paris 5 [UPD5]
Bourdoulous, Sandrine [Auteur]
Université Paris Descartes - Paris 5 [UPD5]
Institut Cochin [UMR_S567 / UMR 8104]
Coureuil, Mathieu [Auteur]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
CHU Necker - Enfants Malades [AP-HP]
Université Paris Descartes - Paris 5 [UPD5]
Journal title :
Proceedings of the National Academy of Sciences
Abbreviated title :
Proc Natl Acad Sci USA
Volume number :
117
Pages :
2606-2612
Publisher :
Proceedings of the National Academy of Sciences
Publication date :
2020-01-21
English keyword(s) :
type IV pili
host–pathogen interaction
virulence
Neisseria meningitidis
glycan
host–pathogen interaction
virulence
Neisseria meningitidis
glycan
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [en]
Bacterial infections are frequently based on the binding of lectin-like adhesins to specific glycan determinants exposed on host cell receptors. These interactions confer species-specific recognition and tropism for ...
Show more >Bacterial infections are frequently based on the binding of lectin-like adhesins to specific glycan determinants exposed on host cell receptors. These interactions confer species-specific recognition and tropism for particular host tissues and represent attractive antibacterial targets. However, the wide structural diversity of carbohydrates hampers the characterization of specific glycan determinants. Here, we characterized the receptor recognition of type IV pili (Tfp), a key adhesive factor present in numerous bacterial pathogens, using Neisseria meningitidis as a model organism. We found that meningococcal Tfp specifically recognize a triantennary sialylated poly-N-acetyllactosamine–containing N-glycan exposed on the human receptor CD147/Basigin, while fucosylated derivatives of this N-glycan impaired bacterial adhesion. Corroborating the inhibitory role of fucosylation on receptor recognition, adhesion of the meningococcus on nonhuman cells expressing human CD147 required prior defucosylation. These findings reveal the molecular basis of the selective receptor recognition by meningococcal Tfp and thereby, identify a potential antibacterial target.Show less >
Show more >Bacterial infections are frequently based on the binding of lectin-like adhesins to specific glycan determinants exposed on host cell receptors. These interactions confer species-specific recognition and tropism for particular host tissues and represent attractive antibacterial targets. However, the wide structural diversity of carbohydrates hampers the characterization of specific glycan determinants. Here, we characterized the receptor recognition of type IV pili (Tfp), a key adhesive factor present in numerous bacterial pathogens, using Neisseria meningitidis as a model organism. We found that meningococcal Tfp specifically recognize a triantennary sialylated poly-N-acetyllactosamine–containing N-glycan exposed on the human receptor CD147/Basigin, while fucosylated derivatives of this N-glycan impaired bacterial adhesion. Corroborating the inhibitory role of fucosylation on receptor recognition, adhesion of the meningococcus on nonhuman cells expressing human CD147 required prior defucosylation. These findings reveal the molecular basis of the selective receptor recognition by meningococcal Tfp and thereby, identify a potential antibacterial target.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Research team(s) :
Génétique des enveloppes bactériennes
Submission date :
2020-07-02T14:57:34Z
2020-07-09T13:51:13Z
2020-07-09T13:51:13Z
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