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2002 | 49 | 2 | 481-490
Article title

Interaction of glycophorin A with lectins as measured by surface plasmon resonance (SPR).

Content
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EN
Abstracts
EN
Glycophorin A (GPA), the major sialoglycoprotein of the human erythrocyte membrane, was isolated from erythrocytes of healthy individuals of blood groups A, B and O using phenol-water extraction of erythrocyte membranes. Interaction of individual GPA samples with three lectins (Psathyrella velutina lectin, PVL; Triticum vulgaris lectin, WGA and Sambucus nigra I agglutinin SNA-I) was analyzed using a BIAcoreTM biosensor equipped with a surface plasmon resonance (SPR) detector. The experiments showed no substantial differences in the interaction between native and desialylated GPA samples originating from erythrocytes of either blood group and each of the lectins. Desialylated samples reacted weaker than the native ones with all three lectins. PVL reacted about 50-fold more strongly than WGA which, similar to PVL, recognizes GlcNAc and Neu5Ac residues. SNA-I lectin, recognizing α2-6 linked Neu5Ac residues, showed relatively weak reaction with native and only residual reaction with desialylated GPA samples. The data obtained show that SPR is a valuable method to determine interaction of glycoproteins with lectins, which potentially can be used to detect differences in the carbohydrate moiety of individual glycoprotein samples.
Publisher

Year
Volume
49
Issue
2
Pages
481-490
Physical description
Dates
published
2002
received
2002-02-07
revised
2002-05-07
accepted
2002-05-21
Contributors
  • Department of Medical Biochemistry, University Medical School, Wrocław, Poland
author
  • Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland
  • Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland
References
  • Endo T, Ohbayashi H, Kanazawa K, Kochibe N, Kobata A. (1992) Carbohydrate binding specificity of immobilized Psathyrella velutina lectin. J Biol Chem.; 267: 707-13.
  • Gallagher JT, Morris A, Dexter TM. (1985) Identification of two binding sites for wheat-germ agglutinin on polylactosamine-type oligosaccharides. Biochem J.; 231: 115-22.
  • Hayashi K. (1975) A rapid determination of sodium dodecyl sulfate with methylene blue. Anal Biochem.; 67: 503-6.
  • Johnsson B, Löfås S, Lindquist G. (1991) Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal Biochem.; 198: 268-77.
  • Jourdian GW, Dean L, Roseman S. (1971) The sialic acids. A periodate-resorcinol method for the quantitative estimation of free sialic acids and their glycosides. J Biol Chem.; 246: 430-5.
  • Kochibe N, Matta KL. (1989) Purification and properties of an N-acetylglucosamine-specific lectin from Psathyrella velutina mushroom. J Biol Chem.; 264: 173-7.
  • Krotkiewski H, Lisowska E, Nilsson G, Grönberg G, Nilsson B. (1993) An improved approach to the analysis of the structure of small oligosaccharides of glycoproteins: application to the O-linked oligosaccharides from human glycophorin A. Carbohydr Res.; 239: 35-50.
  • Krotkiewski H, Duk M, Syper D, Lis H, Sharon N, Lisowska E. (1997) Blood group MN-dependent difference in degree of galactosylation of O-glycans of glycophorin A is restricted to the GalNAc residues located on amino acid residues 2-4 of the glycophorin polypeptide chain. FEBS Lett.; 406: 296-300.
  • Krotkiewska B, Zwierz K, Krotkiewski H. (1999) The carbohydrate moiety of human glycophorin in CDG syndrome. Acta Biochim Polon.; 46: 371-6.
  • Lisowska E. (2001) Antigenic properties of human glycophorin - an update. Adv Exp Med Biol.; 491: 155-69.
  • Lisowska E, Duk M, Dahr W. (1980) Comparison of alkali-labile oligosaccharide chains of M. and N blood-group glycopeptides from human erythrocyte membrane. Carbohydr Res.; 79: 103-13.
  • Lisowska E, Messeter L, Duk M, Czerwiński M, Lundblad A. (1987) A monoclonal anti-glycophorin A antibody recognizing the blood group M. determinant: Studies on the subspecificity. Mol Immunol.; 24: 605-13.
  • Myszka DG, Jonsen MD, Graves BJ. (1998) Equilibrium analysis of high affinity interactions using BIACORE. Anal Biochem.; 265: 326-30.
  • Podbielska M, Krotkiewski H. (2000) Identification of blood group A and B antigens in human glycophorin. Arch Immunol Ther Exp Warsz.; 48: 211-21.
  • Quinn JG, O'Kennedy R, Smyth M, Moulds J, Frame T. (1997) Detection of blood group antigens utilising immobilised antibodies and surface plasmon resonance. J Immunol Methods.; 206: 87-96.
  • Rich RL, Myszka DG. (2000) Survey of the 1999 surface plasmon resonance biosensor literature. J Mol Recognit.; 13: 388-407.
  • Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC. (1985) Measurement of protein using bicinchoninic acid. Anal Biochem.; 150: 76-85.
  • Stenberg E, Persson B, Roos H, Urbaniczky C. (1991) Quantitative determination of surface concentration of protein with surface plasmon resonance by using radiolabeled proteins. J Colloid Interface Sci.; 143: 513-26.
  • Tsuchiya N, Endo T, Matsuta K, Yoshinoya S, Takeuchi F, Nagano Y, Shiota M, Furukawa K, Kochibe N, Ito K, Kobata A. (1993) Detection of glycosylation abnormality in rheumatoid IgG using N-acetylglucosamine-specific Psathyrella velutina lectin. J Immunol.; 151: 1137-46.
  • Ueda H, Kojima K, Saitoh T, Ogawa H. (1999a) Interaction of a lectin from Psathyrella velutina mushroom with N-acetylneuraminic acid. FEBS Lett.; 448: 75- 80.
  • Ueda H, Saitoh T, Kojima K, Ogawa H. (1999b) Multi-specificity of a Psathyrella velutina mushroom lectin: heparin/pectin binding occurs at a site different from the N-acetylglucosamine/N-acetylneuraminic acid-specific site. J Biochem.; 126: 530-7.
  • Van Damme EJM, Barre A, Rouge P, Van Leuven F, Peumans WJ. (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.
  • Wright CS, Kellogg GE. (1996) Differences in hydropathic properties of ligand binding at four independent sites in wheat germ agglutinin-oligosaccharide crystal complexes. Protein Sci.; 5: 1466-76.
  • Yoshima H, Furthmayr H, Kobata A. (1980) Structures of the asparagine-linked sugar chains of glycophorin A. J Biol Chem.; 255: 9713-8.
  • Zdebska E, Musielak M, Jaeken J, Kościelak J. (2001) Band 3 glycoprotein and glycophorin A from erythrocytes of children with congenital disorder of glycosylation type-Ia are underglycosylated. Proteomics.; 1: 269-74.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv49i2p481kz
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