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A Guide for Carbohydrate Specificities of Lectins

  • Chapter
The Molecular Immunology of Complex Carbohydrates

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 228))

Abstract

Lectins are carbohydrate-binding proteins of nonimmune origin, which have been widely used in the fields of cell biology, biochemistry and histochemistry to isolate and/or to characterize cell surface carbohydrates(1–3). Lectins require configurational and structural complementarity of sugars for interaction to occur. All lectin molecules have two or more carbohydrate binding sites, a property essential to their ability to agglutinate cells or to precipitate complex carbohydrates(1, 2, 4). Until the early seventies, the carbohydrate specificities of lectins were mainly determined by the abilities of monosaccharides or their glycosides to inhibit lectin-induced haemagglutination(1, 4). Mäkelä(5), in the late fifties, divided lectin-reactive monosaccharides into four classes, based on their configuration at C-3 and C-4 of the pyranose form, as shown in Fig. 1. Lectins that bind to Mäkelä’s group II sugars are Gal-specific whereas those reacting with sugars of group III are Man and/or Glc-specific lectins. Fucose-binding lectins are specific for group I sugars. Lectins binding sugars belonging to group IV have not yet been reported.

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Abbreviations

Gal:

D-galactopyranose

Glc:

D-glucopyranose

Man:

D-mannopyranose

LFuc or Fuc:

L-fucopyranose

DFuc:

D-fucopyranose

GalNAc:

2-acetamido-2-deoxy-D-galacto-pyranose

GlcNAc:

2-acetamido-2-deoxy-D-gluco-pyranose

chitin oligosaccharide:

(GlcNAcβ1→4)n, repeat unit of GlcNAc

NeuAc:

N-acetylneuraminic acid

NeuGly:

N-glycolylneuraminic acid

R:

carbohydrate residue

Melibiose:

Galα1→6Glc

Raffinose:

Galα1→6Glcβ1→2Fruf

Stachyose:

Galα1→6 Galα1→6Glcβ1→2Fruf

Cellobiose:

Glcβ1→4Glc, and Laminaribiose, Glcβ1→3Glc

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Wu, A.M., Sugii, S., Herp, A. (1988). A Guide for Carbohydrate Specificities of Lectins. In: Wu, A.M., Adams, L.G. (eds) The Molecular Immunology of Complex Carbohydrates. Advances in Experimental Medicine and Biology, vol 228. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1663-3_37

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