Agglutination-induced erythrocyte deformation by two blood group A-specific lectins: studies by light and electron microscopy.

Abstract

The adhesive energy in lectin-induced agglutination can be assessed by the deformation of erythrocytes in aggregates. Helix pomatia (HPA) and Dolichos biflorus (DBA) specifically agglutinated blood group A erythrocytes and induced a change in curvatures of cells at the end of the aggregates. The curvatures changed from concavity to convexity with increasing lectin concentrations. HPA-induced aggregates achieved the theoretical maximal end cell curvature of 0.27 microns-1 at 2-3 micrograms/ml; DBA-induced aggregates approached 0.23 microns-1, requiring 400 micrograms/ml. At any given lectin concentration, HPA showed greater surface binding, caused higher cell curvatures, induced larger aggregate size, and had greater adhesive energies, as compared to DBA. HPA and DBA are globular proteins with a diameter of approximately 5.5 nm and approximately 6.1 nm, respectively, as revealed by the negative staining electron microscopy. The former induced uniform intercellular spacing (approximately 15 nm), whereas the latter induced both smooth (approximately 20 nm) and ruffled spacings. The uniform intercellular spacing was not a function of lectin concentrations. Microscopic studies of erythrocyte deformation provided morphological correlates of biophysical findings of differential adhesive energies induced by these two blood group A-specific lectins.