Cookies Policy

This site uses cookies. By continuing to browse the site you are agreeing to our use of cookies.

I accept this policy

Find out more here

In vitro and in situ localization of concanavalin A and wheat germ agglutinin binding sites on the surface of female cells in Torenia fournieri L.

No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.
The full text of this article is not currently available.

Brill’s MyBook program is exclusively available on BrillOnline Books and Journals. Students and scholars affiliated with an institution that has purchased a Brill E-Book on the BrillOnline platform automatically have access to the MyBook option for the title(s) acquired by the Library. Brill MyBook is a print-on-demand paperback copy which is sold at a favorably uniform low price.

Access this article

+ Tax (if applicable)
Add to Favorites
You must be logged in to use this functionality

image of Israel Journal of Plant Sciences

The interaction between lectins and their specific binding sites is believed to play a critical role in fertilization in animals and some lower plants. However, for higher plants there is no information on lectins or their binding sites related to female gametes and fertilization. The present work was designed as a first attempt to reveal the general pattern of lectin binding site distribution on the surface of female cells, namely egg cells, central cells, and synergids of Torenia fournieri and, especially, to investigate the possible effects of cell isolation procedure on the distribution of lectin binding sites. Therefore, concanavalin A (Con A) and wheat germ agglutinin (WAG) binding sites on the surface of both in vitro and in situ living female cells were localized by using fluorescein isothiocyanate (FITC) conjugated Con A and WGA as probes. We demonstrated that enzymatic treatment and isolation procedures did not notably modify the surface character of the female cells and the distribution of Con A and WGA binding sites. It was also found that Con A binding sites were distributed differently on the surface of the female cells, with the strongest fluorescent signal on central cells and the weakest on egg cells. Calcium could greatly enhance the binding of Con A to the cell surface. A polar distribution pattern of Con A binding sites in embryo sacs was observed. The binding sites were obviously densest at the filiform apparatus of the synergids. The basic pattern of WGA binding site distribution was similar to that of Con A's. However, the fluorescent signal of WGA was much weaker than that of Con A and fluorescent patches were usually found on the cell surface.

Affiliations: 1: Key Laboratory of MOE for Plant Developmental Biology ; 2: Key Laboratory of MOE for Plant Developmental Biology ; 3: Center for Applied Plant Molecular Biology, AMP II, Institute for General Botany, University of Hamburg


Full text loading...


Data & Media loading...

1. Russell, S.D. 1992. Double fertilization. Int. Rev. Cytol. 140: 357-388.
2. Larkin, P.J. 1978. Plant protoplast agglutination by lectins. Plant Physiol. 61: 626-629.
3. Higashiyama, T., Yabe, S., Sasaki, N., Nishimura, Y., Miyagishima, S., Kuroiwa, H., Kuroiwa, T. 2001. Pollen tube attraction by the synergid cell. Science 293: 1480-1483.
4. Hrubá, P., Tupy, J. 1999. N-glycoproteins specific for different stages of microspore and pollen development in tobacco. Plant Sci. 141: 29-40.
5. Johnson, M.H., Eager, D., Muggleton-Harris, A., Grave, H.M. 1975. Mosaicism in organization of concanavalin A receptors on surface membrane of mouse egg. Nature 257: 321- 322.
6. Sun, S., Furtula, V., Nothnagel, E.A. 1992. Mechanical release and lectin labeling of maize root protoplasts. Protoplasma 169: 49-56.
7. Sun, M.X., Kranz, E., Moscatelli, A., Yang, H.Y., Lorz, H., Cresti, M. 2002. A reliable protocol for direct detection of lectin receptors on the plasma membrane of a single living sperm cell in maize. Sex. Plant. Reprod. 15: 53-55.
8. Walko, R.M., Furtula, V., Nothnagel, E.A. 1987. Analysis of labeling of plant protoplast surface by fluorophore-conjugated lectins. Protoplasma 141: 33-46.
9. Wassarman, P.M. 1992. Mouse gamete adhesion molecules. Biol. Reprod. 46: 186-191.
10. Burgess, J., Linstead, P.J. 1976. Ultrastructural studies of the binding of concanavalin A to the plasmalemma of higher plant protoplasts. Planta 130: 73-79.
11. Clarke, A., Gleeson, P., Harrison, S., Knox, R.B. 1979. Pollen- stigma interactions: identification and characterization of surface components with recognition potential. Proc. Natl. Acad. Sci. U.S.A. 76: 3358-3362.
12. El-Husseini, A. E-D., Schnell, E., Dakoji, S., Sweeney, N., Zhou, Q., Prange, O., Gauthier-Campbell, C., Aguilera-Moreno, A., Nicoll, R.A., Bredt, D.S. 2002. Synaptic strength regulated by palmitate cycling on PSD-95. Cell 108: 849-863.
13. Freeman, G. 1996. The role of localized cell surface-associated glycoproteins during fertilization in the Hydrozoan Aequorea. Dev. Biol. 179: 17-26.
14. McCaig, C.D., Robinson, K.R. 1982. The distribution of lectin receptors on the plasma membrane of the fertilized sea urchin egg during first and second cleavage. Dev. Biol. 92: 197-202.
15. Mól, R. 1986. Isolation of protoplasts from female gameto-phytes of Torenia fournieri. Plant Cell. Rep. 3: 202-206.
16. Peumans, W.J., Van Damme, E.J.M. 1995. Lectins as plant defense proteins. Plant Physiol. 109: 347-352.
17. Roth, J. 1978. Compensatory membrane biogenesis and exocytosis as a result of concanavalin A-induced membrane internalization. Exp. Cell. Res. 114: 31-38.
18. Kim, S.H., Kim, G.H. 1999. Cell-cell recognition during fertilization in the red alga, Aglaothamnion oosumiense (Ceramiaceae, Rhodophyta). Hydrobiologia 398/399: 81- 89.
19. Knox, R.B., Clarke, A., Harrison, S., Smith, P., Marchalonis, J.J. 1976. Cell recognition in plants: determinants of the stigma surface and their pollen interactions. Proc. Natl. Acad. Sci. U.S.A. 73: 2788-2792.

Article metrics loading...



Can't access your account?
  • Tools

  • Add to Favorites
  • Printable version
  • Email this page
  • Subscribe to ToC alert
  • Get permissions
  • Recommend to your library

    You must fill out fields marked with: *

    Librarian details
    Your details
    Why are you recommending this title?
    Select reason:
    Israel Journal of Plant Sciences — Recommend this title to your library
  • Export citations
  • Key

  • Full access
  • Open Access
  • Partial/No accessInformation