Skip to main content

Immobilized Lotus tetragonolobus agglutinin binds oligosaccharides containing the Lex determinant

Abstract

A defined set of oligosaccharides and glycopeptides containing α-linked fucose were used to examine the specificity of the immobilized fucose-binding lectin Lotus tetragonolobus agglutinin (LTA1), also known as lotus lectin. Glycans containing the Lewis x determinant (Lex) Galβ1-4[Fucα1-3]GlcNAcβ1-3-R were significantly retarded in elution from high density LTA-Emphaze columns. The lectin also bound the fucosylated lacdiNAc trisaccharide GalNAcβ1-4[Fucα1-3]GlcNAc. The lectin did not bind glycans containing either sialylLex or VIM-2 determinants, nor did it bind the isomeric Lea, Galβ1-3[Fucα1-4]GlcNAc-R. Although 2′-fucosyllactose Fucα1-2Galβ1-4Glc) was retarded in elution from the columns, larger glycans containing the H-antigen Fucα1-2Galβ1-3(4)GlcNAc-R interacted poorly with immobilized LTA. Our results demonstrate that immobilized LTA is effective in isolating glycans containing the Lex antigen and is useful in analyzing specific fucosylation of glycoconjugates. Abbreviations: LTA, Lotus tetragonolobus agglutinin; UEA-1, Ulex europaeus agglutinin-I; LNT, AAL, Aleuria aurantia agglutinin; Galβ1-3GlcNAcβ1-3Galβ1-3Glc; LNnT, Galβ1-4GlcNAcβ1-3Galβ1-3Glc; Lex, Lewis x antigen; Lea, Lewis a antigen; GDPFuc, guanosine 5′-diphosphate-β-L-fucose

This is a preview of subscription content, access via your institution.

References

  1. Goldstein IJ, Hayes CE (1978) Adv Carbohydr Chem Biochem 35: 127–340.

    Google Scholar 

  2. Liener IE, Sharon N, Goldstein IJ, eds (1986) The Lectins: Properties, Functions and Applications in Biology and Medicine. New York: Academic Press.

    Google Scholar 

  3. Lis H, Sharon N (1986) Ann Rev Biochem 55: 35–67.

    Google Scholar 

  4. Osawa T, Tsuji T (1987) Ann Rev Biochem 56: 21–42.

    Google Scholar 

  5. Kobata A, Yamashita K (1993) In Glycobiology: A Practical Approach (Fukuda M, Kobata A, eds) pp. 103–26. Oxford: IRL Press.

    Google Scholar 

  6. Cummings RD (1993) In Glycobiology: A Practical Approach (Fukuda M, Kobata A, eds) pp. 243–90. Oxford: IRL Press.

    Google Scholar 

  7. Cummings RD (1994) Meth Enzymol 230: 66–86.

    Google Scholar 

  8. Matsumoto I, Osawa T (1969) Biochim Biophys Acta 194: 180–9.

    Google Scholar 

  9. Pereira MEA, Kabat EA (1994) Biochemistry 13: 3184–92.

    Google Scholar 

  10. Yamashita K, Kochibe N, Ohkura T, Ueda I, Kobata A (1985) J Biol Chem 260: 4688–93.

    Google Scholar 

  11. Allen HJ, Johnson EAZ, Matta KL (1977) Immunological Communications 6(6): 585–602.

    Google Scholar 

  12. Hindsgaul O, Norberg T, Le Pendu J, Lemieux RU (1982) Carbohydr Res 109: 109–42.

    Google Scholar 

  13. Debray H, Montreuil J (1989) Carbohydr Res 186: 15–26.

    Google Scholar 

  14. Pereira MEA, Kisailus EC, Grueze F, Kabat EA (1978) Arch Biochem Biophys 185: 108–15.

    Google Scholar 

  15. Rosen SD (1994) Curr Opin Cell Biol 6: 663–73.

    Google Scholar 

  16. McEver RP, Moore KL, Cummings RD (1995) J Biol Chem 270: 11025–8.

    Google Scholar 

  17. Solter D, Knowles BB (1978) Proc Natl Acad Sci USA 75: 5565.

    Google Scholar 

  18. Gooi HC, Feizi T, Kapadia A, Knowles BB, Solter D, Evans MJ (1981) Nature 292: 156–8.

    Google Scholar 

  19. Yariv J, Kalb AJ, Blumberg S (1972) Met h Enzymol 28: 356–60.

    Google Scholar 

  20. Lowe JB, Stoolman LM, Nair RP, Larsen RD, Berhend TL, Marks RM (1990) Cell 63: 475–84.

    Google Scholar 

  21. Rajan VP, Larsen RC, Ajmera S, Ernst LK, Lowe JB (1989) J Biol Chem 264: 11158–67.

    Google Scholar 

  22. Kukowska-Latallo JF, Larsen RD, Nair RP, Lowe JB (1990) Gene & Development 4: 1288–303.

    Google Scholar 

  23. DeBose-Boyd R, Nyame AK, Cummings RD (1996) Exp Para-sitol 82: 1–10.

    Google Scholar 

  24. Sueyosh S, Tsuboi S, Sawada-Hirai R, Dang UN, Lowe JB, Fukuda M (1994) J Biol Chem 269: 32342–50.

    Google Scholar 

  25. Merkle RK, Cummings RD (1987) J Biol Chem 262: 8179–89.

    Google Scholar 

  26. Do K-Y, Do S-U, Cummings RD (1995) J Biol Chem 270: 18447–51.

    Google Scholar 

  27. Wilkins PP, McEver RP, Cummings RD (1996) J Biol Chem 271: 18732–42.

    Google Scholar 

  28. Chiu MH, Thomas VH, Stubbs HJ, Rice KG (1995) J Biol Chem 270: 24024–31.

    Google Scholar 

  29. Cummings RD, Kornfeld S (1982) J Biol Chem 257: 11235–40.

    Google Scholar 

  30. Merkle RK, Cummings RD (1987) Meth Enzymol 138: 232–59.

    Google Scholar 

  31. Petryniak J, Goldstein IJ (1986) Biochemistry 25: 2829–38.

    Google Scholar 

  32. Debray H, Decout D, Strecker G, Spik G, Montreuil J (1981) Eur J Biochem 117: 41–55.

    Google Scholar 

  33. Muramatsu T, Gachelin G, Damonneville M, Delarbre C, Jacob F (1979) Cell 18: 183–91.

    Google Scholar 

  34. Bierhuizen MF, Maemura K, Fukuda M (1994) J Biol Chem 269: 4473–9.

    Google Scholar 

  35. Ogata S, Muramatsu T, Kobata A (1975) J Biochem 78: 687–96.

    Google Scholar 

  36. Yamashita K, Tachibana Y, Nakayama T, Kitamura M, Endo Y, Kobata A (1980) J Biol Chem 255: 5635–42.

    Google Scholar 

  37. Lowe JB, Kukowska-Latallo JF, Nair RP, Larsen RD, Marks RM, Macher BA, Kelly RF, Ernst LK (1991) J Biol Chem 266: 17467–77.

    Google Scholar 

  38. Weston BW, Smith PL, Kelly RJ, Lowe JB (1992) J Biol Chem 267: 24575–84.

    Google Scholar 

  39. Kumar R, Potvin B, Muller WA, Stanley P (1991) J Biol Chem 266: 21777–83.

    Google Scholar 

  40. Grinnell BW, Hermann RB, Yan SB (1994) Glycobiology 4: 221–5.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Yan, L., Wilkins, P.P., Alvarez-Manilla, G. et al. Immobilized Lotus tetragonolobus agglutinin binds oligosaccharides containing the Lex determinant. Glycoconj J 14, 45–55 (1997). https://doi.org/10.1023/A:1018508914551

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1018508914551

  • fucosylation
  • Lotus tetragonolobus agglutinin
  • lotus lectin
  • affinity chromatography
  • Lewis antigens