Publications
2009
Mishima Yumiko, Quintin Jessica, Aimanianda Vishukumar, Kellenberger Christine, Coste Franck, Clavaud Cecile, Hetru Charles, Hoffmann Jules A, Latgé Jean-Paul, Ferrandon Dominique, Roussel Alain
The N-terminal domain of Drosophila Gram-negative binding protein 3 (GNBP3) defines a novel family of fungal pattern recognition receptors Article de journal
Dans: J. Biol. Chem., vol. 284, no. 42, p. 28687–28697, 2009, ISSN: 1083-351X.
Résumé | Liens | BibTeX | Étiquettes: Animals, beta-Glucans, Bombyx, Carrier Proteins, Crystallography, ferrandon, Fungal Proteins, Hemolymph, hoffmann, ligands, M3i, Molecular Conformation, Mutagenesis, Polysaccharides, Protein Structure, Secondary, Tertiary, X-Ray
@article{mishima_n-terminal_2009,
title = {The N-terminal domain of Drosophila Gram-negative binding protein 3 (GNBP3) defines a novel family of fungal pattern recognition receptors},
author = {Yumiko Mishima and Jessica Quintin and Vishukumar Aimanianda and Christine Kellenberger and Franck Coste and Cecile Clavaud and Charles Hetru and Jules A Hoffmann and Jean-Paul Latgé and Dominique Ferrandon and Alain Roussel},
doi = {10.1074/jbc.M109.034587},
issn = {1083-351X},
year = {2009},
date = {2009-10-01},
journal = {J. Biol. Chem.},
volume = {284},
number = {42},
pages = {28687--28697},
abstract = {Gram-negative binding protein 3 (GNBP3), a pattern recognition receptor that circulates in the hemolymph of Drosophila, is responsible for sensing fungal infection and triggering Toll pathway activation. Here, we report that GNBP3 N-terminal domain binds to fungi upon identifying long chains of beta-1,3-glucans in the fungal cell wall as a major ligand. Interestingly, this domain fails to interact strongly with short oligosaccharides. The crystal structure of GNBP3-Nter reveals an immunoglobulin-like fold in which the glucan binding site is masked by a loop that is highly conserved among glucan-binding proteins identified in several insect orders. Structure-based mutagenesis experiments reveal an essential role for this occluding loop in discriminating between short and long polysaccharides. The displacement of the occluding loop is necessary for binding and could explain the specificity of the interaction with long chain structured polysaccharides. This represents a novel mechanism for beta-glucan recognition.},
keywords = {Animals, beta-Glucans, Bombyx, Carrier Proteins, Crystallography, ferrandon, Fungal Proteins, Hemolymph, hoffmann, ligands, M3i, Molecular Conformation, Mutagenesis, Polysaccharides, Protein Structure, Secondary, Tertiary, X-Ray},
pubstate = {published},
tppubtype = {article}
}
Gram-negative binding protein 3 (GNBP3), a pattern recognition receptor that circulates in the hemolymph of Drosophila, is responsible for sensing fungal infection and triggering Toll pathway activation. Here, we report that GNBP3 N-terminal domain binds to fungi upon identifying long chains of beta-1,3-glucans in the fungal cell wall as a major ligand. Interestingly, this domain fails to interact strongly with short oligosaccharides. The crystal structure of GNBP3-Nter reveals an immunoglobulin-like fold in which the glucan binding site is masked by a loop that is highly conserved among glucan-binding proteins identified in several insect orders. Structure-based mutagenesis experiments reveal an essential role for this occluding loop in discriminating between short and long polysaccharides. The displacement of the occluding loop is necessary for binding and could explain the specificity of the interaction with long chain structured polysaccharides. This represents a novel mechanism for beta-glucan recognition.