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 UMR 8576 [UGSF]
Leonard, Renaud [Auteur]
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

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 >

Language :

Anglais

Audience :

Non spécifiée

Administrative institution(s) :

Université de Lille
CNRS

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Research team(s) :

Génétique des enveloppes bactériennes

Submission date :

2020-07-02T14:57:34Z
2020-07-09T13:51:13Z