Structure of the Fungal Beta-Glucan-Binding Immune Receptor Dectin-1: Implications for Function.

TLDR: Several dectin‐1 crystal structures are reported, including a high‐resolution structure and a 2.8 Å resolution structure in which a short soaked natural β‐glucan is trapped in the crystal lattice, which suggest potential mechanisms of defense against fungal pathogens.

Abstract: The murine molecule dectin-1 (known as the β-glucan receptor in humans) is an immune cell surface receptor implicated in the immunological defense against fungal pathogens. Sequence analysis has indicated that the dectin-1 extracellular domain is a C-type lectin-like domain, and functional studies have established that it binds fungal β-glucans. We report several dectin-1 crystal structures, including a high-resolution structure and a 2.8 A resolution structure in which a short soaked natural β-glucan is trapped in the crystal lattice. In vitro characterization of dectin-1 in the presence of its natural ligand indicates higher-order complex formation between dectin-1 and β-glucans. These combined structural and biophysical data considerably extend the current knowledge of dectin-1 structure and function, and suggest potential mechanisms of defense against fungal pathogens.