Differential high-affinity interaction of dectin-1 with natural or synthetic glucans is dependent upon primary structure and is influenced by polymer chain length and side-chain branching.

Journal article

Glucans are structurally diverse fungal biopolymers that stimulate innate immunity and are fungal pathogen-associated molecular patterns. Dectin-1 is a C-type lectin-like pattern recognition receptor that binds glucans and induces innate immune responses to fungal pathogens. We examined the effect of glucan structure on recognition and binding by murine recombinant Dectin-1 with a library of natural product and synthetic (1-->3)-beta/(1-->6)-beta-glucans as well as nonglucan polymers. D...

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Authors: Adams, E; Rice, P; Graves, B; Ensley, H; Yu, H

• Publication status: Published
• Journal: Journal of pharmacology and experimental therapeutics
• Volume: 325
• Issue: 1
• Pages: 115-123
• Publication date: 2008-04-01
• DOI: 10.1124/jpet.107.133124
• EISSN: 1521-0103
• ISSN: 0022-3565
• Language: English
• Keywords: Humans; Membrane Proteins; Transfection; Mice; Substrate Specificity; Animals; Immunity, Innate; Ligands; Protein Binding; Mitosporic Fungi; Lectins, C-Type; Yeasts; Carbohydrate Conformation; Nerve Tissue Proteins; Cell Line; beta-Glucans