Quantitative studies of the binding of wheat germ agglutinin (WGA) to chitin-oligosaccharides and partially N-acetylated chitosans suggest inequivalence of binding sites

Carbohydrate Polymers

Volumn 38, Issue 1, 1999, Pages 23-32

  Kristiarisen, Are ^a,b   Nysaæer, Åse ^a   Grasdalen, Hans ^a   Vårum, Kjell M ^a  

^a NORWEGIAN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Norway)

^b Pranova Biomedical   (Norway)

Author keywords

19F NMR spectroscopy; 1H NMR spectroscopy; Binding studies; Chitin; Chitosan; Wheat germ agglutinin (WGA)

Indexed keywords

CHEMICAL BONDS; DEGRADATION; DISSOCIATION; FLUORINE COMPOUNDS; MOLECULAR STRUCTURE; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERS; RATE CONSTANTS; REDUCTION;

TRIFLUOROACETYLGLUCOSAMINE;

CHITIN;

EID: 0032757727     PISSN: 01448617     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0144-8617(98)00106-4     Document Type: Article

References (41)

1. Allen, A.K., Neuberger, A., & Sharon, N. (1973). The purification, composition and specificity of Wheat-Germ Agglutinin. Biochem. J., 131, 155-162.
2. 1H-n.m.r. induced shifts Carbohydr. Polymers, 26, 303-305.
3. 19F magnetic resonance spectroscopic investigation of the binding of 2-deoxy-2-trifluoroacetamido-α-D-glucoseto lysozyme. J. Chem. Soc. D., 10, 512-513.
4. Bains, G., Lee, R.T., Lee, Y.C., & Freire, E. (1992). Microcalorimetric study of Wheat Germ Agglutinin binding to N-acetylglucosamine and its oligomers Biochemistry, 31, 12624-12628.
5. 19F Chemical shifts In NMR Spectroscopy, 2nd ed. (pp. 437-457). San Diego: Academic Press
6. Dahlquist, F.W., & Raftery, M.A. (1968). A nuclear magnetic resonance study of association equilibra and enzyme-bound environments of N-acetyl-D-glucosamine anomers and lysozyme. Biochemistry, 7, 3269-3276.
7. Domard, A., & Cartier, N. (1989). Glucosamine oligomers 1. Preparation and characterization. Int. J. Biol. Macromol., 11, 297-302.
8. Goldstein, I. J. and Poretz, R. D. (1986). Isolation, physicochemical characterization, and carbohydrate-binding specificity of lectins In I. E. Liener, N. Sharon and I. J. Goldstein (Eds), The Lectins (pp. 33-247). Orlando, FL: Academic Press
9. Goldstein, I.J., Hammarstrøm, S., & Sundblad, G. (1975). Precipitation and carbohydrate-binding specificity studies on wheat germ agglutinin. Biochim. Biophys Acta, 405, 53-61.
10. Hahn, M.G. (1996). Microbial elicitors and their receptors in plants Annu. Rev. Phytopathol., 34, 387-412.
11. Harata, K., Nagahora, H., & Jigami, Y. (1995). X-ray structure of Wheat Germ Agglutinin Isolectin 3. Acta Cryst. D, 51, 1013-1019.
12. Jordan, F., Bassett, E., & Redwood, W.R. (1977). Proton magnetic resonance studies on wheat germ agglutinin-amino sugar interaction. Evidence for involvement of a tryptophan residue in the binding process Biochem. Biophys Res Comm., 75, 1015-1021.
13. Jordan, F., Bahr, H., Patrick, J., & Woo, P.W.K. (1981). Nuclear magnetic resonance studies on Wheat Germ Agglutinin - monomeric amino sugar interactions Arch. Bioch. Biophys, 207, 81-86.
14. Kronis, K.A., & Carver, J.P. (1982). Specificity of isolectins of Wheat Germ Agglutinin for sialyloligosaccharides A 360-M Hz proton nuclear magnetic resonance binding study. Biochemistry, 21, 3050-3057.
15. Kronis, K.A., & Carver, J.P. (1985). Wheat Germ Agglutinin dimers bind sialyloligosaccharides at four sitesin solution: Proton nuclear magnetic resonance temperature studies at 360 MHz. Biochemistry, 24, 826-833.
16. Lotan, R., & Sharon, N. (1973). The fluorescence of wheat germ agglutinin and of its complexes with saccharides Biochem. Biophys Res Comm., 55, 1340-1346.
17. Lotan, R., Sharon, N., & Mirelman, D. (1975). Interaction of Wheat-Germ Agglutinin with bacterial cells and cell-wall polymers Eur. J. Biochem., 55, 257-262.
18. Monsigny, M., Sene, C., Obrenovitch, A., Roche, A.-C., Delmotte, F., & Boschetti, E. (1979). Properties of succinylated Wheat-Germ Agglutinin. Eur. J. Biochem., 98, 39-45.
19. Nagata, Y., & Burger, M.M. (1974). Wheat Germ Agglutinin. Molecular characteristics and specificity for sugar binding. J. Biol. Chem., 249, 3116-3122.
20. Peumans, W.J., & van Damme, E.J.M. (1995). Lectins as plant defence proteins Plant Physiol., 109, 347-352.
21. Privat, J.-P., Delmotte, F., Mialonier, G., Bouchard, P., & Monsigny, M. (1974). Fluorescence studies of saccharide binding to Wheat Germ Agglutinin. Eur. J. Biochem., 47, 5-14.
22. Privat, J.-P., Delmotte, F., & Monsigny, M. (1974). Protein-sugar interactions Association of β(1-4) linked N-acetyl-D-glucosamine oligomer derivatives with wheat germ agglutin in (lectin). FEBS Lett., 46, 224-228.
23. Raikhel, N.V., Lee, H.I., & Broekaert, W.F. (1993). Structure and function of chitin-binding proteins Annu. Rev. Plant Physiol. Plant Mol. Biol., 44, 591-615.
24. Rice, R.H., & Etzler, M.E. (1974). Subunit structure of Wheat Germ Agglutinin. Biochem. Biophys Res Comm, 59, 414-419.
25. Rice, R.H., & Etzler, M.E. (1975). Chemical modifications and hybridization of Wheat Germ Agglutinin. Biochemistry, 14, 4093-4099.
26. Sannan, T., Kurita, K., & Iwakura, Y. (1976). Studies on chitin, 2. Effect of deacetylation on solubility. Makromol. Chem., 177, 3589-3600.
27. Senstad, C., & Mattiasson, B. (1988). Purification of Wheat Germ Agglutinin using affinity flocculation with chitosan and a subsequent centrifugation or flotation step. Biotechn. Bioeng., 34, 387-393.
28. Varum, K.M., Anthonsen, M.W., Grasdalen, H., & Smidsrød, O. (1991). Determination of the degree of N-acetylation and the distribution of N-acetyl groups in partially N-deacetylated chitins (chitosans) by high-field n.m.r. spectroscopy. Carbohydr. Res, 211, 17-23.
29. 13C-N.m.r. studies of the acetylation sequences in partially N-deacetylated chitins (chitosans). Carbohydr. Res, 217, 19-27.
30. Varum, K.M., Ottøy, M.H., & Smidsriød, O. (1994). Water-solubility of partially N-acetylated chitosans as a function of pH: Effect of chemical composition and depolymerisation. Carbohydr. Polymers, 25, 65-70.
31. Weis, W.I., & Drickamer, K. (1996). Structural basis of lectin-carbohydrate recognition. Annu. Rev. Biochem., 65, 441-473.
32. 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR, 6, 135-140.
33. Wright, C.S. (1980). Crystallographic elucidation of the saccharide binding mode in Wheat Germ Agglutinin and its biological significance. J. Mol. Biol., 141, 267-291.
34. Wright, C.S. (1984). Structural comparisons of the two distinct sugar binding sites in Wheat Germ Agglutinin isolectin II. J. Mol. Biol., 178, 91-104
35. Wright, C.S. (1990). 2.2 A° resolution structure analysis of two refined N-acetylneur aminyl-lactose-Wheat Germ Agglutinin isolectin complexes J. Mol. Biol., 215, 635-651.
36. Wright, C.S. (1992). Crystal structure of a Wheat Germ agglutinin/ glycophorin-sialoglycopeptide receptor complex. J. Biol. Chem., 267, 14345-14352.
37. Wright, C.S., & Kellogg, G.E. (1996). Differences in hydropathic properties of ligand binding at four independent sites in wheat germ agglutinin-oligosacchari de complex es Protein Sci., 5, 1466-1476.
38. Wright, C.S., & Olafsdottir, S. (1986). Structural differences in the two major Wheat Germ Agglutinin isolectins J. Biol. Chem., 261, 7191-7195.
39. Wright, C.S., & Raikhel, N. (1989). Sequence variability in three Wheat Germ Agglutinin isolectins Products of multiple genes in polyploid wheat. J. Mol. Evol., 28, 327-336.
40. Wright, H.T., Sandrasegaram, G., & Wright, C.S. (1991). Evolution of a family of N-acetyl glucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin. J. Mol. Evol., 33, 283-294.
41. Wüthrich, K. (1986). NMR of Proteinsand Nucleic Acids New York: John Wiley & Sons Inc.