Cell agglutination mediated by concanavalin A and the dynamic state of the cell surface.

The binding of I-labelled concanavalin A (I-Con A) to the cell surface has been studied in Ehrlich ascites tumour cells (EATC) and beef erythrocytes under various conditions. The binding of concanavalin A (Con A) to the cell surface was very specific and the available binding sites were saturated within a few minutes. The amount of I-Con A bound to EATC was 4-14 x io molecules/cell at 37 °C and 212 x io molecules/cell at o °C. Under these conditions, cell agglutination was observed only at 37 °C and not at o °C. However, the binding sites measured at o °C were also effective for agglutination at 37 °C. Beef erythrocytes were agglutinated by Con A only after treatment of cells with papain. The number of binding sites for Con A on the cell surface was decreased by this treatment to about half the number present on untreated cells. Various reagents such as colchicine, monoiodoacetic acid, dinitrophenol, rotenone, sodium azide and carboxyl cyanide-m-fluorophenylhydrazone (FCCP) had no effect on Con A-mediated cell agglutination. In contrast, periodate treatment produced a remarkable decrease in the agglutinability of cells. From these data, it is concluded that the cell agglutination induced by Con A was due to the topographical distribution of the surface receptors for the lectin, and not the result of energy-dependent or microtubule-dependent reaction processes. The number and the state of Con A receptors on the cell surface were in a dynamic condition, their conformation, orientation, and/or topographical distribution changing under different conditions.