YAKHAK HOEJI (약학회지)

The Pharmaceutical Society of Korea (대한약학회)
권호 표지

Neutral and Amino Sugars Composition of a Lectin from Maackia fauriei

Maackia fauriei 유래 렉틴의 중성당 및 아미노당 조성

  • Published : 2009.02.28
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Abstract

The glycosylation of therapeutic glycoproteins can affect their efficacy, stability, solubility, and half-life. Analyzing the composition of monosaccharides, such as that of neutral and amino sugars, is the first step for elucidating the structure of glycan attached to glycoproteins. In the present study, neutral and amino sugars of lectin obtained from Maackia fauriei were analyzed using an enzyme-linked lectinsorbent assay (ELLA) and high-performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD). Peroxidase-labeled lectins such as concanavalin A, Ricinus communis agglutinin, and soybean agglutinin were used for ELLA, since they specifically bind to the monosaccharide residue most frequently encountered in a glycan. The hydrosylate of lectin was prepared by treatment with trifluoroacetic acid, which resulted in the lectin mainly possessing the N-glycan consisting of 98.1 pmol Fuc, 342.1 pmol GlcN, 51.9 pmol Gal, 678.9 pmol Man, and 330.7 pmol Xyl. The present results demonstrate that ELLA and HPAEC-PAD are very effective methods for rapidly estimating the types and relative amounts of monosaccharides in intact glycoproteins.

Keywords

References

  1. Wyss, D. F. and Wagner, G. : The structural role of sugars in glycoproteins. Curr. Opin. Biotech. 7, 409 (1996) https://doi.org/10.1016/S0958-1669(96)80116-9
  2. Lisowska, E. : The role of glycosylation in protein antigenic properties. Cell. Mol. Life Sci. 59, 445 (2002) https://doi.org/10.1007/s00018-002-8437-3
  3. Matsumoto, S. : Characterization of a human glycoprotein(erythropoietin) produced in cultured tobacco cells. Plant Mol. Biol. 27, 1163 (1995) https://doi.org/10.1007/BF00020889
  4. Sairam, M. R. : Role of carbohydrates in glycoprotein hormone signal transduction. FASEB J. 3, 1915 (1989)
  5. Sinclair, A. M. and Elliott, S. : Glycoengineering : The effect of glycosylation on the properties of therapeutic proteins. J. Pharm. Sci. 94, 1626 (2005) https://doi.org/10.1002/jps.20319
  6. Dube, S., Fisher, J. W. and Powell, J. S. : Glycosylation at specific sites of erythropoietin is essential for biosynthesis, secretion, and biological function. J. Biol. Chem. 263, 17516(1988)
  7. Liu, T. Y. : Natural and biotech-derived therapeutic proteins : What is the future ? Electrophoresis 21, 1914 (2000) https://doi.org/10.1002/(SICI)1522-2683(20000501)21:9<1914::AID-ELPS1914>3.0.CO;2-U
  8. Ueda, H. and Ogawa, H : Glycobiology of the plant glycoprotein epitope : structure, immunogenicity and allergenicity of plant glycotopes. Trends Glycosci. Glyc. 11, 413 (1999) https://doi.org/10.4052/tigg.11.413
  9. Rumpel, C. and Dignac, M. : Gas chromatographic analysis of monosaccharides in a forest soil profile : analysis by gas chromatography after trifluoroacetic acid hydrolysis and reduction–acetylation. Soil Biol. Biochem. 38, 1478 (2006) https://doi.org/10.1016/j.soilbio.2005.09.017
  10. Cataldi, T. R. I. and Campa, C. : Carbohydrate analysis by highperformance anion exchange chromatography with pulsed amperometric detection : The potential still growing. J. Anal. Chem. 368, 739 (2000) https://doi.org/10.1007/s002160000588
  11. Guttman, A : Analysis of monosaccharide composition by capillary electrophoresis. J. Chromatogr. A 763, 271 (1997) https://doi.org/10.1016/S0021-9673(96)00750-9
  12. Wu, W., Hamase, K., Kiguchi, M., Yamamoto, M. and Zaitsu, K. : Reversed-phase HPLC of monosaccharides in glycoproteins derivatized with aminopyrazine with fluorescence detection. Anal. Sci. 16, 919 (2000) https://doi.org/10.2116/analsci.16.919
  13. Jahnel, J. B. Ilieva, P. and Frimmel, F. H. : HPAEC-PAD-a sensitive method for the determination of carbohydrates. Fresen. J. Anal. Chem. 360, 827 (1998) https://doi.org/10.1007/s002160050819
  14. Lee, Y. C. : Carbohydrate analyses with high-performance anion-exchange chromatography. J. Chromatogr. A 720, 137(1996) https://doi.org/10.1016/0021-9673(95)00222-7
  15. Kim, B. S., Oh, K. T., Cho, D. H., Kim, Y. J., Koo, W. M., Kong, K. H. and Kim, H. H. : A sialic acid-binding lectin from the legume Maackia fauriei : comparison with lectins from M. amurensis. Plant Sci. 167, 1315 (2004) https://doi.org/10.1016/j.plantsci.2004.06.029
  16. Laemmli, U. K. : Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680(1970) https://doi.org/10.1038/227680a0
  17. Bradford, M. M. : A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248(1976) https://doi.org/10.1016/0003-2697(76)90527-3
  18. Leriche, V., Sibille, P. and Carpentier, B. : Use of an enzymelinked lectinsorbent assay to monitor the shift in polysaccharide composition in bacterial biofilms. Appl. Environ. Microbiol. 66, 1851 (2000) https://doi.org/10.1128/AEM.66.5.1851-1856.2000
  19. Baenziger, J. V. and Fiete, D. : Structure of the complex oligosaccharides of fetuin. J. Biol. Chem. 254, 789 (1979)
  20. Gunther, G. R., Wang, J. L., Yahara, I., Cunningham, B. A. and Edelman, G. M. : Concanavalin A derivatives with altered biological activities. Proc. Natl. Acad. Sci. 70, 1012 (1973) https://doi.org/10.1073/pnas.70.4.1012
  21. Lin, T. T. and Li, S. L. : Purification and physicochemical properties of ricins and agglutinins from Ricinus communis. Eur. J. Biochem. 105, 453-459 (1980) https://doi.org/10.1111/j.1432-1033.1980.tb04520.x
  22. Lotan, R., Siegelman, H. W., Lis, H. and Sharon, N. : Subunit structure of soybean agglutinin. J. Biol. Chem. 249, 1219(1974)
  23. Karakasa, I. I., Iwase, H. and Hotta, K. : Structural determination of the O-linked sialyl oligosaccharides liberated from fetuin with endo-$\alpha$-N-acetylgalactosaminidase-S by HPLC analysis and 600-MHz 1H-NMR spectroscopy. Eur. J. Biochem. 247, 709 (2004) https://doi.org/10.1111/j.1432-1033.1997.00709.x
  24. Nilsson, B. and Svensson, S. : Structural studies on the carbohydrate portion of fetuin. J. Biol. Chem. 254, 4545 (1979)
  25. Kim, S., Kim, S. I., Ha, K. S. and Leem, S. H. : An improves method for quantitative sugar analysis of glycoproteins. Exp. Mol. Med. 32, 141 (2000) https://doi.org/10.1038/emm.2000.24
  26. Currie, H. A. and Perry, C. C. : Resolution of complex monosaccharide mixtures from plant cell wall isolates by high pH anion exchange chromatography. J. Chromatogr. A 1128, 90(2006) https://doi.org/10.1016/j.chroma.2006.06.045
  27. Aubery, M., Reynier, M., Lopez, M., Ogier-Denis, E., Font, J. and Bardin, F. : WGA binding to the surface of two autologous human melanoma cell lines: different expression of sialyl and N-acetylglucosaminyl residues. Cell. Biol. Int. Rep. 14, 275(1990) https://doi.org/10.1016/S0309-1651(05)80010-4
  28. Mody, R., Joshi, S. and Chaney, W. : Use of lectin as diagnostic and therapeutic tools for cancer. J. Pharmacol. Toxicol. 33, 1(1995)