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

E. P. McGreal, M. Rosas, G. D. Brown, S. Zamze, Simon Yuk Chun Wong, S. Gordon, L. Martinez-Pomares, P. R. Taylor

Research output: Contribution to journalArticle

218 Citations (Scopus)

Abstract

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 (Man(9)GlcNAc(2)). 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.

Original languageEnglish
Pages (from-to)422-430
Number of pages8
JournalGlycobiology
Volume16
DOIs
Publication statusPublished - 2006

Keywords

  • lectin
  • macrophage
  • mannose
  • MARGINAL ZONE MACROPHAGES
  • DC-SIGN
  • BINDING PROTEIN
  • DENDRITIC CELLS
  • SELECTIVE RECOGNITION
  • ENDOTHELIAL-CELLS
  • MEDIATES UPTAKE
  • HOST-DEFENSE
  • HUMAN-IGG
  • IN-VIVO

Cite this

McGreal, E. P., Rosas, M., Brown, G. D., Zamze, S., Wong, S. Y. C., Gordon, S., ... Taylor, P. R. (2006). The carbohydrate-recognition domain of Dectin-2 is a C-type lectin with specificity for high mannose. Glycobiology, 16, 422-430. https://doi.org/10.1093/glycob/cwj077

The carbohydrate-recognition domain of Dectin-2 is a C-type lectin with specificity for high mannose. / McGreal, E. P.; Rosas, M.; Brown, G. D.; Zamze, S.; Wong, Simon Yuk Chun; Gordon, S.; Martinez-Pomares, L.; Taylor, P. R.

In: Glycobiology, Vol. 16, 2006, p. 422-430.

Research output: Contribution to journalArticle

McGreal, EP, Rosas, M, Brown, GD, Zamze, S, Wong, SYC, Gordon, S, Martinez-Pomares, L & Taylor, PR 2006, 'The carbohydrate-recognition domain of Dectin-2 is a C-type lectin with specificity for high mannose' Glycobiology, vol. 16, pp. 422-430. https://doi.org/10.1093/glycob/cwj077
McGreal, E. P. ; Rosas, M. ; Brown, G. D. ; Zamze, S. ; Wong, Simon Yuk Chun ; Gordon, S. ; Martinez-Pomares, L. ; Taylor, P. R. / The carbohydrate-recognition domain of Dectin-2 is a C-type lectin with specificity for high mannose. In: Glycobiology. 2006 ; Vol. 16. pp. 422-430.
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abstract = "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 (Man(9)GlcNAc(2)). 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.",
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AU - McGreal, E. P.

AU - Rosas, M.

AU - Brown, G. D.

AU - Zamze, S.

AU - Wong, Simon Yuk Chun

AU - Gordon, S.

AU - Martinez-Pomares, L.

AU - Taylor, P. R.

PY - 2006

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N2 - 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 (Man(9)GlcNAc(2)). 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.

AB - 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 (Man(9)GlcNAc(2)). 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.

KW - lectin

KW - macrophage

KW - mannose

KW - MARGINAL ZONE MACROPHAGES

KW - DC-SIGN

KW - BINDING PROTEIN

KW - DENDRITIC CELLS

KW - SELECTIVE RECOGNITION

KW - ENDOTHELIAL-CELLS

KW - MEDIATES UPTAKE

KW - HOST-DEFENSE

KW - HUMAN-IGG

KW - IN-VIVO

U2 - 10.1093/glycob/cwj077

DO - 10.1093/glycob/cwj077

M3 - Article

VL - 16

SP - 422

EP - 430

JO - Glycobiology

JF - Glycobiology

SN - 0959-6658

ER -