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Glycobiology Advance Access originally published online on January 19, 2006
Glycobiology 2006 16(5):422-430; 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

The carbohydrate-recognition domain of Dectin-2 is a C-type lectin with specificity for high mannose

Eamon P. McGreal2,6, Marcela Rosas6, Gordon D. Brown3,6, Susanne Zamze7, Simon Y.C. Wong4,7, Siamon Gordon6, Luisa Martinez-Pomares5,6 and Philip R. Taylor1,6

2 Present address: Department of Child Health, Wales College of Medicine, University of Cardiff, Heath Park, Cardiff CF14 4XN, UK
3 Present address: Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Lower Ground Floor, Wernher & Beit Building South, Groote Schuur Campus, Observatory, 7925, Cape Town, South Africa
4 Present address: School of Molecular Medical Sciences, University of Nottingham, Floor A, West Block, Queen’s Medical Centre, Nottingham NG7 2UH, UK
5 Present address: Inflammation and Immunity Theme, Department 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; and 7 The Edward Jenner Institute for Vaccine Research, Compton, Berkshire RG20 7NN, UK

1 To whom correspondence should be addressed; e-mail: philip.taylor{at}path.ox.ac.uk

Received on November 16, 2005; revised on January 11, 2006; accepted on January 12, 2006

We examined the carbohydrate-binding potential of the C-type lectin-like receptor Dectin-2 (Clecf4n). The carbohydrate-recognition domain (CRD) 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 CRD exhibited only weak interactions to some of these capsular polysaccharides, indicative of different structural or affinity requirements for binding, when compared with 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 the specificity of these three mannose-specific lectins indicate that mannose recognition is mediated by distinct receptors, with unique specificity, that are expressed by discrete subpopulations of cells, and this further highlights the complex nature of carbohydrate recognition by immune cells.

Key words: lectin / macrophage / mannose


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