Structure of the Fungal Beta-Glucan-Binding Immune Receptor Dectin-1: Implications for Function.
James Brown,Christopher A. O’Callaghan,Andrew S J Marshall,Robert J.C. Gilbert,Christian Siebold,Siamon Gordon,Gordon D. Brown,E Y Jones +7 more
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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.read more
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Identification of the porcine C-type lectin Dectin-1
TL;DR: The porcine dectin-1 was identified and characterized in the pig as discussed by the authors, and two major isoforms (GenBank acc. no. FJ386383 and FJ 386384) were identified by the presence of a stalk region separating the carbohydrate recognition domain from the transmembrane region.
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Macrophage specific delivery of TNF-α siRNA complexed with β-1,3-glucan inhibits LPS-induced cytokine production in a murine acute hepatitis model.
TL;DR: A novel complex consisting of β-1,3-glucan and short interference RNA (siRNA) and a siRNA that is designed to suppress tumor necrosis factor alpha (TNF-α) and shows higher affinity to recombinant dectin-1 than SPG itself, which may overcome the problem for RNA interference therapy because of its non-toxicity and high target specificity.
Journal ArticleDOI
Effects of dietary levan on growth performance, nonspecific immunity, pathogen resistance and body composition of orange‐spotted grouper (Epinephelus coioides H.)
Mei-Ying Huang,Mei-Ying Huang,Chin-I Chang,Chih-Chien Chang,Liang-Wei Tseng,Chorng-Liang Pan +5 more
TL;DR: The results of this study indicate that dietary levan (25.0 g kg−1) could be an effective method for enhancing the growth performance and disease resistance in orange-spotted grouper.
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Identification and characterization of Cryptosporidium parvum Clec, a novel C-type lectin domain-containing mucin-like glycoprotein.
Seema Bhalchandra,Jacob G. Ludington,Jacob G. Ludington,Isabelle Coppens,Honorine D. Ward,Honorine D. Ward +5 more
TL;DR: The identified C. parvum Clec, a novel mucin-like glycoprotein that contains a C-type lectin domain (CTLD) and has orthologs in C. hominis and C. muris, strongly implicate a significant role for CpClec in Cryptosporidium-host cell interactions.
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Probing β-(1→3)-d-glucans interactions with recombinant human receptors using high-resolution NMR studies
Balla Sylla,Jean-Paul Guégan,Jean-Paul Guégan,Jean-Michel Wieruszeski,Caroline Nugier-Chauvin,Caroline Nugier-Chauvin,Laurent Legentil,Laurent Legentil,Richard Daniellou,Richard Daniellou,Vincent Ferrières,Vincent Ferrières +11 more
TL;DR: A full characterization of the high-resolution NMR spectrum of the laminarihexaose is described and used for the determination of the binding epitope of the more complex but structurally related laminarin.
References
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