Survey of a receptor protein in human erythrocytes for hemagglutinin of Porphyromonas gingivalis.

The purpose of this study is to survey a receptor protein in human erythrocyte membrane for the hemagglutinin (HA) of Porphyromonas gingivalis. Human erythrocytes were modified by either chymotrypsin or P. gingivalis HA along with the disappearance of their hemagglutinating ability and the removal of the band 3 protein. By preparative electrophoresis, this protein was isolated and purified from human erythrocytes. The purified protein showed strong inhibitory activity for hemagglutination and the binding to P. gingivalis cells, whose binding sites were calculated to be approximately 9000, suggesting its binding to the active site of HA. Hemagglutinin purified from P. gingivalis by affinity absorption to sheep erythrocyte ghosts possessed strong trypsin-like activity, and both the HA and the enzyme activities were inhibited by arginine. Specific modification of arginyl residues in human erythrocytes by phenylglyoxal diminished the hemagglutinating ability. From the similarity of the inhibition profile and possible active sites between HA and the trypsin-like protease, it is suggested that hemagglutination may occur as a result of the primary reaction of the enzyme (protease) and the substrate. These results suggest that band 3 may be a key protein in human erythrocyte membrane for HA from P. gingivalis and its binding sites may be arginyl residues of the protein.