Characterization of the Human β-Glucan Receptor and Its Alternatively Spliced Isoforms

Janet A. Willment, Siamon Gordon, Gordon D. Brown*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

287 Scopus citations

Abstract

β-1,3-D-Glucans are biological response modifiers with potent effects on the immune system. A number of receptors are thought to play a role in mediating these responses, including murine Dectin-1, which we recently identified as a β-glucan receptor. In this study we describe the characterization of the human homologue of this receptor and show that it is structurally and functionally similar to the mouse receptor. The human β-glucan receptor is a type II transmembrane receptor with a single extracellular carbohydrate recognition domain and an immunoreceptor tyrosine activation motif in its cytoplasmic tail. The human β-glucan receptor is widely expressed and functions as a pattern recognition receptor, recognizing a variety of β-1,3- and/or β-1,6-linked glucans as well as intact yeast. In contrast to the murine receptor, the human receptor mRNA is alternatively spliced, resulting in two major (A and B) and six minor isoforms. The two major isoforms differ by the presence of a stalk region separating the carbohydrate recognition domain from the transmembrane region and are the only isoforms that are functional for β-glucan binding. The human receptor also binds T-lymphocytes at a site distinct from the β-glucan binding site, indicating that this receptor can recognize both endogenous and exogenous ligands.

Original languageEnglish
Pages (from-to)43818-43823
Number of pages6
JournalJournal of Biological Chemistry
Volume276
Issue number47
DOIs
StatePublished - 23 11 2001
Externally publishedYes

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