Plant Biol (Stuttg) 2005; 7(5): 501-508
DOI: 10.1055/s-2005-865854
Research Paper

Georg Thieme Verlag Stuttgart KG · New York

Polar Distribution Dynamics of Con A Binding Sites in Embryo Sacs is Temporally Coupled by the Fertilization Process

K. F. Fang1 , T. T. Yan1 , M. X. Sun1
  • 1Key Laboratory of MOE for Plant Developmental Biology, College of Life Science, Wuhan University, Wuhan 430072, China
Further Information

Publication History

Received: January 9, 2005

Accepted: June 2, 2005

Publication Date:
15 September 2005 (online)


The binding site distribution of concanavalin agglutinin (Con A) and wheat germ agglutinin (WGA) on embryo sacs at various developmental stages of Torenia fournieri L was studied by using a cooled Charge Coupled Device (CCD) and fluorescent Con A and WGA probes. The distribution patterns of Con A and WGA binding sites on embryo sacs changed during the fertilization process. The fluorescent signal indicating Con A binding sites was distributed evenly on the surface of the embryo sac wall before anthesis, was much denser on the micropylar end of the embryo sac wall and looked like a corona on the day of anthesis. After pollination, stronger fluorescence was present on the micropylar end of the embryo sac wall and the filiform apparatus (FA), showing an obvious polar distribution. When the pollen tube entered the embryo sac and reached a synergid, the fluorescence was still concentrated on the micropylar end and FA, and started to appear on the synergid. After fertilization, the polar distribution of the fluorescence gradually disappeared and an even distribution pattern was observed again on the embryo sac wall. These results revealed that the dynamic distribution of Con A binding sites was temporally coupled with the process of fertilization. WGA binding site distribution on the embryo sac was also investigated and showed a simple pattern but also regularly changed during the process of fertilization. The variation of these lectin binding sites during the fertilization process suggests that lectin binding site interactions may play a role in the process.


M. X. Sun

Key Laboratory of MOE for Plant Developmental Biology
College of Life Science
Wuhan University

Wuhan 430072



Editor: S. M. Wick