Survey of immune-related, mannose/fucose-binding C-type lectin receptors reveals widely divergent sugar-binding specificities

Reiko T. Lee, Tsui Ling Hsu, Shau Ku Huang, Shie Liang Hsieh, Chi Huey Wong, Yuan C. Lee

Research output: Contribution to journalArticle

76 Citations (Scopus)

Abstract

C-type lectins (CTLs) are proteins that contain one or more carbohydrate-recognition domains (CRDs) that require calcium for sugar binding and share high degree of sequence homology and tertiary structure. CTLs whose CRD contain EPN (Glu-Pro-Asn) tripeptide motifs have potential to bind mannose (Man), N-acetylglucosamine (GlcNAc), glucose (Glc) and l-fucose (Fuc), whereas those with QPD (Glu-Pro-Asp) tripeptide motifs bind galactose (Gal) and N-acetylgalactosamine (GalNAc). We report here for the first time a direct comparison of monosaccharide (and some di- and trisaccharides)-binding characteristics of 11 EPX-containing (X = N, S or D) immune-related CTLs using a competition assay and an enzyme-linked immunosorbent assay, and neoglycoproteins as ligand. The EPX CTLs studied are DC-SIGN, L-SIGN, mSIGNR1, human and mouse mannose receptors, Langerin, BDCA-2, DCIR, dectin-2, MCL and MINCLE. We found that: (1) they all bound Man and Fuc; (2) binding of Glc and GlcNAc varied considerably among these lectins, but was always less than Man and Fuc; (3) in general, Gal and GalNAc were not bound. However, dectin-2, DCIR and MINCLE showed ability to bind Gal/GalNAc; (4) DC-SIGN, L-SIGN, mSIGNR1 and Langerin showed enhanced binding of Man2Man over Man, whereas all others showed no enhancement; (5) DC-SIGN bound Lex trisaccharide structure, which has terminal Gal and Fuc residues, more avidly than Fuc, whereas L-SIGN, mSIGNR1, DCIR and MINCLE bound Lex less avidly than Fuc. BDCA-2, dectin-2, Langerin, MCL and mannose receptor did not bind Lex at all.

Original languageEnglish
Pages (from-to)512-520
Number of pages9
JournalGlycobiology
Volume21
Issue number4
DOIs
Publication statusPublished - Apr 1 2011
Externally publishedYes

Fingerprint

C-Type Lectins
Fucose
Mannose
Galactose
Acetylgalactosamine
Sugars
Trisaccharides
Assays
Carbohydrates
Glucose
Immunosorbents
Acetylglucosamine
Monosaccharides
Disaccharides
Sequence Homology
Lectins
Glycoproteins
Enzyme-Linked Immunosorbent Assay
Ligands
Calcium

Keywords

  • binding specificity
  • C-type lectin
  • immune receptor
  • mannose/fucose-binding

ASJC Scopus subject areas

  • Biochemistry

Cite this

Survey of immune-related, mannose/fucose-binding C-type lectin receptors reveals widely divergent sugar-binding specificities. / Lee, Reiko T.; Hsu, Tsui Ling; Huang, Shau Ku; Hsieh, Shie Liang; Wong, Chi Huey; Lee, Yuan C.

In: Glycobiology, Vol. 21, No. 4, 01.04.2011, p. 512-520.

Research output: Contribution to journalArticle

Lee, Reiko T. ; Hsu, Tsui Ling ; Huang, Shau Ku ; Hsieh, Shie Liang ; Wong, Chi Huey ; Lee, Yuan C. / Survey of immune-related, mannose/fucose-binding C-type lectin receptors reveals widely divergent sugar-binding specificities. In: Glycobiology. 2011 ; Vol. 21, No. 4. pp. 512-520.
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