HEMAGGLUTINATION ACTIVITY OF LACTOBACILLUS-ACIDOPHILUS GROUP LACTIC-ACID BACTERIA

The cells of 28 strains of the Lactobacillus acidophilus group were ev aluated for hemagglutination (HA) activity. The activity was found in the surface layer (SL) protein fraction extracted by 2M guanidine hydr ochloride. The most SL proteins from the A group strains (L. acidophil us (A(1)), L. crispatus (A(2)), L. amylovorus (A(3)), and L. gallinaru m (A(4))) showed HA activity, but the proteins from the B group strain s (L. gasseri (B-1) and L. johnsonii (B-2)) showed no activity. The SL proteins from the A group strains were composed in common of a main c omponent having molecular mass of about 40-45 kDa on SDS-PAGE. The SL proteins from JCM 1034 strain that showed the highest HA activity was fractionted by CM-Toyopearl ion-exchange chromatography. The highest H A activity was detected in the major protein of 41 kDa. This protein w as purified and shown to be composed of about 50% of hydrophobic amino acids. The HA activity of the protein (1034 lectin) was specifically inhibited by fetuin and bovine lactoferrin at the concentrations of 80 and 160 mu g/ml, respectively. The removal of N-acetylneuraminic acid from fetuin significantly decreased the inhibitory activity.