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Glycobiology Advance Access published online on January 19, 2006
Glycobiology, doi:10.1093/glycob/cwj077
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received November 16, 2005
Revised January 11, 2006
Accepted January 12, 2006

Article

The Carbohydrate Recognition Domain of Dectin-2 is a C-Type Lectin with Specificity for High-Mannose

Eamon P. McGreal 1, Marcela Rosas 2, Gordon D. Brown 3, Susanne Zamze 4, Simon Y.C. Wong 5, Siamon Gordon 2, Luisa Martinez-Pomares 6, and Philip R. Taylor 2 *

1 Sir William Dunn School of Pathology, Oxford University, South Parks Road, Oxford, OX1 3RE, UK; Department of Child Health, Wales College of Medicine, University of Cardiff, Heath Park, Cardiff, CF14 4XN, UK
2 Sir William Dunn School of Pathology, Oxford University, South Parks Road, Oxford, OX1 3RE, UK
3 Sir William Dunn School of Pathology, Oxford University, South Parks Road, Oxford, OX1 3RE, UK; Institute of Infectious Disease and Molecular Medicine, Faculty of Health Sciences, University of Cape Town, Lower Ground Floor, Wernher & Beit Building South, Groote Schuur Campus, Observatory, 7925, Cape Town, South Africa
4 The Edward Jenner Institute for Vaccine Research, Compton, Berkshire, RG20 7NN, UK
5 The Edward Jenner Institute for Vaccine Research, Compton, Berkshire, RG20 7NN, UK; Inflammation and Immunity Theme, Dept. of Medicine and Therapeutics, University of Aberdeen, Foresterhill, Aberdeen, Scotland AB25 2ZD, UK
6 Sir William Dunn School of Pathology, Oxford University, South Parks Road, Oxford, OX1 3RE, UK; School of Molecular Medical Sciences, University of Nottingham, Floor A, West Block, Queen’s Medical Centre, Nottingham, NG7 2UH, UK

* To whom correspondence should be addressed.
Philip R. Taylor, E-mail: philip.taylor{at}path.ox.ac.uk


  Abstract

We have examined the carbohydrate binding potential of the C-type lectin-like receptor Dectin-2 (Clecf4n). The carbohydrate recognition domain of Dectin-2 exhibited cation-dependent mannose/fucose-like lectin activity with an IC50 for mannose of approximately 20 mM compared to an IC50 of 1.5 mM for the macrophage mannose receptor when assayed by similar methodology. The extracellular domain of Dectin-2 exhibited binding to live Candida albicans and the Saccharomyces-derived particle zymosan. This binding was completely abrogated by cation-chelation and was competed by yeast mannans. We compared the lectin activity of Dectin-2 with that of two other C-type lectin receptors (mannose receptor and SIGNR1) known to bind fungal mannans. Both mannose receptor and SIGNR1 were able to bind bacterial capsular polysaccharides derived from Streptococcus pneumoniae but interestingly they exhibited distinct binding profiles. The Dectin-2 carbohydrate recognition domain exhibited only weak interactions to some of these capsular polysaccharides indicative of different structural or affinity requirements for binding, when compared to the other two lectins. Glycan array analysis of the carbohydrate recognition by Dectin-2 indicated specific recognition of high mannose structures (Man9GlcNAc2). The differences in specificity of these three ‘mannose-specific’ lectins indicate that ‘mannose-recognition’ is mediated by distinct receptors, with unique specificity, which are expressed by discrete subpopulations of cells and this further highlights the complex nature of carbohydrate recognition by immune cells.

Keywords: Lectin/Macrophage/Mannose.
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