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Concanavalin A pp 13–33Cite as

Structure and Function of Concanavalin A

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 55))

Abstract

Lectins have been extensively used to analyze a variety of fundamental processes in cell biology. In conjuntion with our studies on the cell surface and mitosis, we have determined the amino acid sequence and three-dimensional struction of concanavalin A (Con A), the mitogenic lectin from the jack bean. Knowledge of the structure has been helpful in interpreting experiments on lymphocyte mitogenesis and the effects of Con A on cell surface receptor mobility.

Con A subunits of molecular weight 25,500 are folded into dome-like structures of maximum dimensions 42 x 40 x 39 Å. The domes are related by 222 symmetry to form roughly tetrahedral tetra-mers. Each subunit contains two large antiparallel pleated sheets, and subunits are joined to form dimers and tetramers by interactions involving one of these pleated sheets. We have examined the binding of a variety of carbohydrates to Con A and have obtained preliminary data which suggest that there are differences in the saccharidebinding behavior of Con A in solution and in the crystalline state.

Dimeric chemical derivatives of Con A have been prepared and shown to have biological activities different from those of the native tetrameric protein. Under different conditions, native Con A exhibits two antagonistic activities on the lymphoid cell surface: the induction of cap formation by its own receptors and the inhibition of the mobility of a variety of receptors, including its own receptors. The dimeric derivative, succinyl-Con A, is just as effective a mitogen as the native lectin, but it lacks the ability to modulate cell surface receptor mobility: The data suggest that neither extensive immobilization of cell surface receptors nor cap formation is required for cell stimulation. Further studies on modulation of receptor translocation suggest the hypothesis that there exists a connecting network of colchicine-sensitive proteins that links receptors, of different kinds and mediates their rearrangement. The degree of connectivity of this postulated network appears to be altered by changes in the state of attachment of various surface receptors to the network. Thus the network might provide the cell with a means of transmitting signals such as the stimulus for mitosis by lectins or antigens.

This work was supported by grants from the National Institutes of Health, the National Science Foundation, and a Teacher-Scholar Grant from the Camille and Henry Dreyfus Foundation. J. L. Wang is a Fellow of the Damon Runyon Memorial Fund for Cancer Research.

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References

  1. Barber, B. H., Quirt, A., and Carver, J. P. (1975). “Magnetic resonance studies of concanavalin A: Location of the binding site of a-methyl-D-mannopyranoside.” This book, p. 325.

    Google Scholar 

  2. Barnett, R. E., Scott, R. E., Furcht, L. T., and Kersey, J. H. (1974). “Evidence that mitogenic lectins induce changes in lymphocyte membrane fluidity.” Nature 249, 465.

    Article  PubMed  CAS  Google Scholar 

  3. Becker, J. W., Reeke, G. N., and Edelman, G. M. (1971). “Location of the saccharide-binding site of concanavalin A.” J. BioZ. Chem. 246, 6123.

    CAS  Google Scholar 

  4. Becker, J. W., Reeke, G. N., Wang, J. L., Cunningham, B. A., and Edelman, G. M. (1974). “The covalent and three-dimensional structure of concanavalin A. III. Structure of the monomer and its interactions with metals and saccharides.” J. BioZ. Chem., submitted for publication.

    Google Scholar 

  5. Beckert, W. H., and Sharkey, M. M., Sr. (1970). “Mitogenic activity of the jack bean (Canavalia ensiformis) with rabbit peripheral blood lymphocytes.” Int. Arch. Allergy and Appt. Immunol. 39, 337.

    Article  CAS  Google Scholar 

  6. Berlin, R. D., Oliver, J. M., Ukena, T. E., and Yin, H. H. (1974). “Control of cell surface topography.” Nature 247, 45.

    Article  PubMed  CAS  Google Scholar 

  7. Brewer, C. F., Sternlicht, H., Marcus, D. M., and Grollman, A. P. (1973a). “Binding of 13C-enriched a-methyl-D-glucopyranoside to concanavalin A as studied by carbon magnetic resonance.” Proc. Nat. Acad. Sci. U.S.A. 70, 1007.

    Article  CAS  Google Scholar 

  8. Brewer, C. F., Sternlicht, H., Marcus, D. M., and Grollman, A. P. (1973b). “Interactions of saccharides with concanavalin A. Mechanism of binding of a-and ß-methyl-D-glucopyranoside to concanavalin A as determined by 13C nuclear magnetic resonance.” Biochemistry 12, 4448.

    Article  PubMed  CAS  Google Scholar 

  9. Brewer, C. F., Sternlicht, H., Marcus, D. M., and Grollman, A. P. (1975). “C NMR studies of the interaction of concanavalin A with saccharides.” This book, p. 55.

    Google Scholar 

  10. DePetris, S., Raff, M. C., and Mallucci, L. (1973). “Ligand-induced redistribution of concanavalin A receptors on normal, trypsinized, and transformed fibroblasts.” Nature New Biol. 244, 276.

    Article  Google Scholar 

  11. Edelman, G. M., Cunningham, B. A., Reeke, G. N., Becker, J. W., Waxdal, M. J., and Wang, J. L. (1972). “The covalent and three-dimensional structure of concanavalin A.” Proc. Nat. Acad. Sci. U.S.A. 69, 2580.

    Article  CAS  Google Scholar 

  12. Edelman, G. M., Yahara, I., and Wang, J. L. (1973). “Receptor mobility and receptor-cytoplasmic interactions in lymphocytes.” Proc. Nat. Acad. Sci. U.S.A. 70, 1442.

    Article  CAS  Google Scholar 

  13. Fox, T. 0., Sheppard, J. R., and Burger, M. M. (1971). “Cyclic membrane changes in animal cells: Transformed cells permanently display a surface architecture detected in normal cells only during mitosis.” Proc. Nat. Acad. Sci. U.S.A. 68, 244.

    Article  CAS  Google Scholar 

  14. Gunther, G. R., Wang, J. L., Yahara, I., Cunningham, B. A., and Edelman, G. M. (1973). “Concanavalin A derivatives with altered biological activities.” Proc. Nat. Acad. Sci. U.S.A. 70, 1012.

    Article  CAS  Google Scholar 

  15. Gunther, G. R., Wang, J. L., and Edelman, G. M. (1974). “The kinetics of cellular commitment during stimulation of lymphocytes by lectins.” J. Cell Biol.,in press.

    Google Scholar 

  16. Goldstein, I. J., Hollerman, C. E., and Smith, E. E. (1965). “Protein-carbohydrate interaction. II. Inhibition studies on the interaction of concanavalin A with polysaccharides.” Biochemistry 4, 876.

    Article  PubMed  CAS  Google Scholar 

  17. Goldstein, I. J., Reichert, C. M., and Misaki, A. (1974). “Interaction of concanavalin A with model substrates.” Ann. N.Y. Acad. Sci.,in press.

    Google Scholar 

  18. Hardman, K. D., Wood, M. K., Schiffer, M., Edmundson, A. B., and Ainsworth, C. F. (1971a). “X-ray crystallographic studies of concanavalin A.” Cold Spring Harbor Symp. Quant. BioZ. 36, 271.

    Article  CAS  Google Scholar 

  19. Hardman, K. D., Wood, M. K., Schiffer, M., Edmundson, A. B., and Ainsworth, C. F. (1971b). “Structure of concanavalin A at 4.25Xngstrom resolution.” Proc. Nat. Acad. Sci. U.S.A. 68, 1393.

    Article  CAS  Google Scholar 

  20. Hardman, K. D., and Ainsworth, C. F. (1972). “Structure of concanavalin A at 2.4 X resolution.” Biochemistry 11,. 4910.

    Google Scholar 

  21. Hardman, K. D. and Ainsworth, C. F. (1973). “Binding of non-polar molecules by crystalline concanavalin A.” Biochemistry 12, 4442.

    Article  PubMed  CAS  Google Scholar 

  22. Inbar, M., and Sachs, L. (1969). “Interaction of the carbohydrate-binding protein concanavalin A with normal and transformed cells.” Proc. Nat. Acad. Sci. U.S.A. 63, 1418.

    Article  CAS  Google Scholar 

  23. Inbar, M., Ben-Bassat, H., and Sachs, L. (1972). “Membrane changes associated with malignancy.” Nature New Biol. 236, 3, 16.

    Google Scholar 

  24. Kalb, A. J., and Levitzki, A. (1968). “Metal-binding sites of concanavalin A and their role in the binding of a-methyl-Dglucopyranoside.” Biochem. J. 109, 669.

    PubMed  CAS  Google Scholar 

  25. Kalb, A. J., and Lustig, A. (1968). “The molecular weight of concanavalin A.” Biochim. et Biophys. Acta 168–366.

    Google Scholar 

  26. Nicolson, G. L. (1971). “Different distribution of ferritinconjugated concanavalin A on surfaces of normal and tumor cell membranes.” Nature New BioZ. 233, 244.

    CAS  Google Scholar 

  27. Nicolson, G. L., and Singer, S. J. (1971). “Ferritin-conjugated plant agglutinins as specific saccharide stains for electron microscopy: Application to saccharides bound to cell membranes.” Proc. Nat. Acad. Sci. U.S.A. 68, 942.

    Article  CAS  Google Scholar 

  28. Ozanne, B., and Sambrook, J. (1971). “Binding of radioactively labelled concanavalin A and wheat germ agglutinin to normal and virus-transformed cells.” Nature New BioZ. 232 156.

    Google Scholar 

  29. Pflumm, M. N. Wang, J. L., and Edelman, G. M. (1971). “Conformational changes in concanavalin A.” J. BioZ. Chem. 246, 4369.

    Google Scholar 

  30. Poretz, R. D., and Goldstein, I. J. (1970). “An examination of the topography of the saccharide binding sites of concanavalin A and of the forces involved in complexation.” Biochemistry 9, 2890.

    Article  PubMed  CAS  Google Scholar 

  31. Powell, A. E., and Leon, M. A. (1970). “Reversible interaction of human lymphocytes with the mitogen concanavalin A.” ExptZ. CeZZ Res. 62, 315.

    Article  CAS  Google Scholar 

  32. Quiocho, F. A. and A resolution., Reeke, G. N., Becker, J. W., Lipscomb, W. N., G. M. (1971). “Structure of concanavalin A at 4 ” Proc. Nat. Acad. Sci. U.S.A. 68, 1853.

    Article  CAS  Google Scholar 

  33. Reeke, G. N., structure of Harbor Symp. Becker, J. W., and Quiocho, F. A. (1971). “The concanavalin A at 4 X resolution.” Cold Spring Quant. Biol. 36, 277.

    Google Scholar 

  34. Rosenblith, J. Z., Ukena, T. E., Yin, H. H., Berlin, R. D., and Karnovsky, M. J. (1973). “A comparative evaluation of the distribution of concanavalin A binding sites on the surfaces of normal, virally-transformed, and protease-treated fibroblasts.” Proc. Nat. Acad. Sci. U.S.A. 70, 1625.

    Article  CAS  Google Scholar 

  35. Rutishauser, U., Yahara, I., and Edelman, G. M. (1974). “Morphology, motility, and surface behavior of lymphocytes bound to nylon fibers.” Proc. Nat. Acad. Sci. U.S.A. 71, 1149.

    Article  CAS  Google Scholar 

  36. So, L. L., and Goldstein, I. J. (1967). “Protein-carbohydrate interaction. IX. Application of the quantitative hapten inhibition technique to polysaccharide-concanavalin A interaction. Some comments on the forces involved in concanavalin A-polysaccharide interaction.” J. Immunol. 99, 158.

    PubMed  CAS  Google Scholar 

  37. So, L. L., and Goldstein, I. J. (1969). “Protein-carbohydrate interaction. XXI. The interaction of concanavalin A with Dfructans.” Carbohyd. Res. 10, 231.

    Article  CAS  Google Scholar 

  38. Sumner, J.B. (1919). ‘”the globulins of the jack bean, Canavalia ensiformis.” J. Biol. Chem. 37 137.

    Google Scholar 

  39. Sumner, J. jack bean 29, 133. B. (1919). “The globulins of the jack bean, ensiformis.” J. BioZ. Chem. 37, 137.

    CAS  Google Scholar 

  40. Sumner, J. B., and Howell, S. F. (1936a). “The identification of the hemagglutinin of the jack bean with concanavalin A.” J. Bacteriol. 32, 227.

    PubMed  CAS  Google Scholar 

  41. Sumner, J. B., and Howell, S. F. (1936b). “The role of divalent metals in the reversible inactivation of jack bean hemagglutinin.” J. BioZ. Chem. 115, 583.

    CAS  Google Scholar 

  42. Taylor, R. B., Duffus, P. H., Radd, M. C., and DePetris, S. (1971). “Redistribution and pinocytosis of lymphocyte surface immunoglobulin molecules induced by anti-immunoglobulin antibody.” Nature New BioZ. 233, 225.

    CAS  Google Scholar 

  43. Unanue, E. R., Perkins, W. D., and Karnovsky, M. J. (1972). “Ligand-induced movement of lymphocyte membrane macromolecules. I. Analysis by immunofluorescence and ultrastructural radiography.” J. ExptZ. Med. 136, 885.

    Article  CAS  Google Scholar 

  44. Villafranca, J. J., and Viola, R. E. (1974). “The use of 13C spin lattice relaxation times to study the interaction of amethyl-D-glucopyranoside with concanavalin A.” Arch. Biochem. Biophys. 160, 465.

    Article  PubMed  CAS  Google Scholar 

  45. Wang, J. L., Cunningham, B. A., and Edelman, G. M. (1971). “Unusual fragments in the subunit structure of concanavalin A.” Proc. Nat. Acad. Sci. U.S.A. 68, 1130.

    Article  CAS  Google Scholar 

  46. Wilson, L., and Friedkin, M. (1967). “The biochemical events of mitosis. II. The in vivo and in vitro binding of colchicine in grasshopper embryos and its possible relation to inhibition of mitosis.” Biochemistry 6, 3126.

    Article  PubMed  CAS  Google Scholar 

  47. Yahara, I., and Edelman, G. M. (1972). “Restriction of the mobility of lymphocyte immunoglobulin receptors by concanavalin A.” Proc. Nat. Acad. Sci. U.S.A. 69, 608.

    Article  CAS  Google Scholar 

  48. Yahara, I., and Edelman, G. M. (1973a). “The effects of concanavalin A on the mobility of lymphocyte surface receptors.” ExptZ. CeZZ Res. 81, 143.

    Article  CAS  Google Scholar 

  49. Yahara, I., and Edelman, G. M. (1973b). “Modulation of lymphocyte receptor redistribution by concanavalin A, anti-mitotic agents, and alterations of pH.” Nature 246, 152.

    Article  PubMed  CAS  Google Scholar 

  50. Young, N. M. (1974). “The effects of maleylation on the properties of concanavalin A.” Biochim. et Biophys. Acta 336 46.

    Google Scholar 

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Author information

Authors and Affiliations

  1. The Rockefeller University, New York, New York, USA

    George N. Reeke Jr., Joseph W. Becker, Bruce A. Cunningham, John L. Wang, Ichiro Yahara & Gerald M. Edelman

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  1. George N. Reeke Jr.
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  2. Joseph W. Becker
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  4. John L. Wang
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  6. Gerald M. Edelman
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Editors and Affiliations

  1. Department of Physiology and Biophysics, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA

    Tushar K. Chowdhury  & A. Kurt Weiss  & 

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© 1975 Plenum Press, New York

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Reeke, G.N., Becker, J.W., Cunningham, B.A., Wang, J.L., Yahara, I., Edelman, G.M. (1975). Structure and Function of Concanavalin A. In: Chowdhury, T.K., Weiss, A.K. (eds) Concanavalin A. Advances in Experimental Medicine and Biology, vol 55. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-0949-9_2

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  • DOI: https://doi.org/10.1007/978-1-4684-0949-9_2

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