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The Molecular Immunology of Complex Carbohydrates pp 205–263Cite as

Differential Binding Properties of GalNAc and/or Gal Specific Lectins

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

Abstract

The binding properties of lectins have been used to study the structural and functional role of cell surface carbohydrates (1–6), to detect sugar moieties on normal and neoplastic cell surfaces (1), to isolate mutants resistant to the cytotoxic action of some lectins (7–10), and to isolate and characterize glycoconjugates (5, 11–13A). This group of lectins generally recognize D-pyranose sugars, and require configurational and structural complementarity of sugars for interaction to occur. All lectin molecules have more than two carbohydrate binding sites, a property resulting in their ability to agglutinate cells or to precipitate complex carbohydrates (1,4,14,15). Until the early seventies, the carbohydrate specificities of lectins, were determined by the ability of monosaccharides or their glycosides to inhibit lectin-induced hemagglutination (2,14,17,18). In the early eighties, lectins of the same apparent monosaccharide specificity were found to demonstrate different reactivities toward different oligosaccharide chains, and differential affinities to animal cells and glycoproteins, implying that they have their own binding specificity extending beyond the monosaccharide (1–4,14,18).

This paper is dedicated to Dr. A. Herp, who has assisted my research for a decade.

Some of the content in this review article, especially the section related t o Galß1→3 GalNAc specific lectins, has been published in Mol. Cell. Bio chem., 61:131–141, 1984 and is reproduced with permission by Martinus Nijhoff publisher, Boston.

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Abbreviations

Gal:

D-galactopyranose

Glc:

D-glucopyranose

Man:

D-mannopyranose

LFuc:

L-fucopyranose

GalNAc:

2-acetamido-2-deoxy-Dgalactopyranose

GlcNAc:

2-acetamido-2-deoxy-D-glucopyranose; (GlcNAcß1→4) n repeating unit of GlcNAcß1→4GlcNAc

NeuAc:

N-acetylneuraminicacid

R:

carbohydrate residues; Melibiose Galαl→6Glc

Raffinose, Galαl→6Glcß1→2Fruf:

Stachyose Galαl→6Galαl→6Glcß1→2Fruf

BGS:

blood group active glycoproteins (substances)

QPA:

Quantitative precipitin assay

QPIA:

Quantitative precipitin-inhibition assay

F:

GaINAcαl→3GaINAc

A:

GaINAcαl→3Gal

Af:

GalNAcαl→3 [LFucαl→2] Gal related

T:

Galß1→3GalNAcαl→Ser (Thr) of proteincore or Galß1→3GaINAcß1→ at the terminal nonreducing end of the ganglioside

Tn:

GaINAcαl→Ser(Thr) of the peptide chain

I(II):

Human blood groups type I and II carbohydrate sequence, Galß1→3(4)GlcNAc at the nonreducing end of the carbohydrate chain (17A)

B:

Galßl→3Gal at the nonreducing end of the carbohydrate chain

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Authors and Affiliations

  1. Department of Veterinary Pathology, College of Veterinary Medicine, Texas A&M University, College Station, 77843, TX, USA

    Albert M. Wu

  2. Department of Serology and Immunology, School of Medical Technology, Kitasato University, 1-15-1 Kitasato, 228, Sagamihara, Kanagawa, Japan

    Shunji Sugii

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  1. Texas Agricultural Experimental Station, Texas A&M University, College Station, Texas, USA

    Albert M. Wu  & L. Garry Adams  & 

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Wu, A.M., Sugii, S. (1988). Differential Binding Properties of GalNAc and/or Gal Specific 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_9

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  • DOI: https://doi.org/10.1007/978-1-4613-1663-3_9

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