Abstract
Glycosylation has been recognized as one of the most important modifications on proteins. The interactions between proteins and glycans are known to play an important role in many biological processes. Lectins are carbohydrate-binding proteins that can specifically interact with and select for carbohydrate structures. The technique of lectin affinity chromatography takes advantage of this specific interaction and enables the selection and purification of glycoproteins with carbohydrate structures complementary to the lectin-binding site. Depending on the carbohydrate specificity of the lectin glycoprotein fractions enriched for example, high mannose or complex N-glycans or O-glycans can be obtained. Afterward both the protein part and the glycan part can be analyzed in more detail allowing the identification of the interacting partners and the type of glycans involved.
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References
Van Damme, E. J. M., Peumans, W. J., Barre, A., and Rougé, P. (1998) Plant lectins: a composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles. Crit Rev Plant Sci 17, 575–692.
Van Damme, E. J. M., Peumans, W. J., Pusztai, A., and Bardocz, S. (1998) Handbook of Plant Lectins: Properties and Biomedical Applications, John Wiley & Sons, Chichester, p. 452.
Van Damme, E. J. M., Rougé, P., and Peumans, W. J. (2007) Plant lectins. In: Comprehensive Glycoscience – From Chemistry to Systems Biology, J. P. Kamerling, G. J. Boons, Y. C. Lee, A. Suzuki, N. Taniguchi, and A. J. G. Voragen, eds., Elsevier, New York, volume 3, pp. 563–99.
Van Damme, E. J. M., Lannoo, N., and Peumans, W. J. (2008) Plant lectins. Adv Bot Res 48, 107–209.
Van Damme, E. J. M., Smith, D. F., Cummings, R., and Peumans, W. J. (2011) Glycan arrays to decipher the specificity of plant lectins. In: The Molecular Immunology of Complex Carbohydrates, A. M. Wu, ed., Kluwer Academic/Plenum Publishers, New York, 841–854.
Taylor, M. E. and Drickamer, K. (2009) Structural insights into what glycan arrays tell us about how glycan-binding proteins interact with their ligands. Glycobiology 19, 1155–62.
Yue, T. and Haab, B. B. (2009) Microarrays in glycoproteomics research. Clin Lab Med 29, 15–29.
Blixt, O., Head, S., Mondala, T., Scanlan, C., Huflejt, M. E., Alvarez, R., et al. (2004) Printed covalent glycan array for ligand profiling of diverse glycan binding proteins. Proc Natl Acad Sci USA 101, 17033–38.
Paulson, J. C., Blixt, O., and Collins, B. E. (2006) Sweet spots in functional glycomics. Nat Chem Biol 2, 238–48.
Hirabayashi, J. (2008) Concept, strategy and realization of lectin-based glycan profiling. J Biochem 144, 139–47.
Pilobello, K. T., Krishnamoorthy, L., Slawek, D., and Mahal, L. K. (2005) Development of a lectin microarray for the rapid analysis of protein glycopatterns. Chembiochem 6, 985–9.
Van Damme, E. J. M., Allen, A. K., and Peumans, W. J. (1987) Isolation and characterization of a lectin with exclusive specificity towards mannose from snowdrop (Galanthus nivalis) bulbs. FEBS Lett 215, 140–4.
Van Damme, E. J. M., Barre, A., Rougé, P., Van Leuven, F., and Peumans, W. J. (1996) The NeuAc (α-2,6)-Gal/GalNAc binding lectin from elderberry (Sambucus nigra) bark, a type 2 ribosome inactivating protein with an unusual specificity and structure. Eur J Biochem 235, 128–37.
Wang, W.-C. and Cummings, R. D. (1988) The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex type Asn-linked oligosaccharides containing terminal sialic acid-linked α-2,3 to penultimate galactose residues. J Biol Chem 261, 4576–85.
Chen, Y., Peumans, W. J., Hause, B., Bras, J., Kumar, M., Proost, P., et al. (2002) Jasmonic acid methyl ester induces the synthesis of a cytoplasmic/nuclear chitooligosaccharide-binding lectin in tobacco leaves. FASEB J 16, 905–7.
Vranken, A. M., Van Damme, E. J. M., Allen, K., and Peumans, W. J. (1987) Purification and properties of an N-acetyl-galactosamine specific lectin from the plant pathogenic fungus Rhizoctonia solani. FEBS Lett 216, 67–72.
Bador, M., Cabrera, G., Stadlmann, J., Lerouge, P., Cremata, J. A., Gomord, V., et al. (2009) N-glycosylation of plant recombinant pharmaceuticals. In: Recombinant Proteins from Plants, Methods and Protocols, Springer Protocols, L. Faye and V. Gomord, eds., Humana Press, New York, pp. 239–64.
Lihme, A., Schafer-Nielsen, C., Larsen, K. P., Müller, K. G., and Bøg-Hansen, T. C. (1986) Divinylsulphone-activated agarose. Formation of stable and non-leaking affinity matrices by immobilization of immunoglobulins and other proteins. J Chromatogr 376, 299–305.
Shibuya, N., Goldstein, I. J., Van Damme, E. J. M., and Peumans, W. J. (1988) Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb. J Biol Chem 263, 728–34.
Lannoo, N., Peumans, W. J., Van Pamel, E., Alvarez, R., Xiong, T.-C., Hause, G., et al. (2006) Localization and in vitro binding studies suggest that the cytoplasmic/nuclear tobacco lectin can interact in situ with high-mannose and complex N-glycans. FEBS Lett 580, 6329–37.
Shibuya, N., Goldstein, I. J., Broekaert, W. F., Nsimba-Lubaki, M., Peeters, B., and Peumans, W. J. (1987) The elderberry (Sambucus nigra) bark lectin recognizes the Neu5Ac (α2-6)/GalNAc sequence. J Biol Chem 262, 1596–601.
Shibuya, N., Goldstein, I. J., Broekaert, W. F., Nsimba-Lubaki, M., Peeters, B., and Peumans, W. J. (1987) Fractionation of sialylated oligosaccharides, glycopeptides and glycoproteins on immobilized elderberry (Sambucus nigra) bark lectin. Arch Biochem Biophys 254, 1–8.
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The financial support of the Research Council of Ghent University and Fund for Scientific Research-Flanders (G.0022.08) is gratefully acknowledged.
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Van Damme, E.J.M. (2011). Lectins as Tools to Select for Glycosylated Proteins. In: Gevaert, K., Vandekerckhove, J. (eds) Gel-Free Proteomics. Methods in Molecular Biology, vol 753. Humana Press. https://doi.org/10.1007/978-1-61779-148-2_19
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DOI: https://doi.org/10.1007/978-1-61779-148-2_19
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