Roles of the structural units, glycotopes / mammalian N-glycans for Con A - Glycan interactions, their codes, and their recognition Factors-Reference-Cited by-同舟云学术

Roles of the structural units, glycotopes / mammalian N-glycans for Con A - Glycan interactions, their codes, and their recognition Factors

Published:2023-02-06 Issue: Volume: Page:
ISSN:
Container-title:
language:
Short-container-title:

Author:

Wu Albert M.¹

Affiliation:

1. Chang Gung University

Abstract

Abstract The binding property of Con A has been studied intensively and applied widely to glycoconjugates / glycobiology for over 80 years. However, its role and functional relationship of Con A with these mammalian structural units, glycotopes, N-glycan chains, as well as their polyvalent forms in N-glycoproteins involved in the Con A- glycan interactions have not been all defined and organzied. In this study, the recognition factors involved in these inteactions were azalyzed by our well developed method- the enzyme linked lectinosorbent (ELLSA) and inhibition assay. Based on all data obtained, it is concluded that Con A, as previous report, has a relatively broad and wide recognition ability with the Manα1→ and Glcα1→ related glycans. In addition to it reacted strongly with yeast mannan and glycogens, it also bound well with a large number of mammalian N-glycans, including the N-glycans of rat sublingual gp (RSL), human Tamm-Horsfall glycoprotein (THGP), thyroglobin and lactosferrin. The recognition specificity of Con A towards ligands, expressed by Molar Relative Potency (Molar R.P.), in a decreasing order is as follows: a1→3, a1→6 Mannopentaose (M5) and Biantennary N-linked core pentasaccharide (MDi) ≥ a1→3, a1→6 Mannotriose (M3) > Mana1→3Man (α1→3Mannobiose), Mana1→2Man (α1→2Mannobiose), Mana1→6Man (α1→6Mannobiose), Mana1→4Man (α1→4Mannobiose) > GlcNAcb1→2Man (b1→2 N-Acetyl glucosamine-mannose) > Mana1→/Glcα1→ > Man > Glc, while Gal / GalNAc were inactive. Furthermore, the Man related code system, in this study, is proposed to express by both numbers of Man and GlcNAcb1→ branches (M3 to M9 / MMono to Penta etc.) and a table of three Mana1→ and Glca1→ related biomasses of six recognition factors involved in the Con A-glycan interactions has also been demonstrated. These themes should be one of the most valuable advances since 1980s.

Publisher

Research Square Platform LLC

Reference64 articles.

1. Goldstein, I.J., Poretz, R.D.: Isolation, physicochemical characterization, and carbohydrate-binding specificity of lectins. In: Liener, I.E., Sharon, N., Goldstein, I.J. (eds.) The lectins: properties, functions, and applications in biology and medicine. Chapter 2, pp. 35–244. Orlando Academic Press (1986)

2. Goldstein, I.J., Winter, H.C., Poretz, R.D.: Plant lectins: tools for the study of complex carbohydrates. In: Montreuil, J., Vliegenthart, J.F.G. and Schachter, H. (eds.) Glycoproteins II. New comprehensive biochemistry, Vol. 29b, Chap. 12, pp. 403–470. Elsevier Science B. V., Amsterdam (1997)

3. Sharon, N., Lis, H.: Specificity and affinity. In: Sharon, N., Lis, H. (eds.) Lectins, pp. 63–103. Kluwer Academic Publishers, Dordrecht, The Netherlands (2003). Chap. 4

4. Lectins as Cell Recognition Molecules;Sharon N;Science.,1989

5. Wu, A.M., Sugii, S.J., Herp, A.: A Guide for Carbohydrate specificities of Lectins. In: Wu, A.M. (ed.) The Molecular Immunology of Complex Carbohydrates. Adv. Exp. Med. Biol. 228, the appendix, pp. 817–853. Plenum Press, New York and London (1988)