HEMAGGLUTININ PROTEIN 35.7 kDA ACTS AS AN ADHESION MOLECULE IN THE OUTER MEMBRANE PROTEIN (OMP) OF SHIGELLA DYSENTERIAE

Shigellosis becomes a major health problem of developing countries. It is caused by Shigella spp. Shigella dysenteriae causes the most severe; prolonged and fatal Shigellosis by its ability in producing Shigatoxin (Stx). Unfortunately, there has not been any effective vaccine available in worldwide and using antibiotic is no longer effective. Adhesion molecule of bacteria can be used as component of vaccine as its facilitates attachment into host in which the adhesion molecule located in Outer Membrane Protein (OMP). This research aims to confirm the molecular weight (MW) of OMP’s sub unit protein that acts as an adhesion molecule of S.dysenteriae. OMP was isolated using NOG 0.05% and profiled using SDS PAGE. Dominant sub unit protein was purificated using electroelution method. According to Hemagglutinin Assay (HA), sub unit protein with MW 35.47 kDa has the ability to agglutinate mice eritrocyte in the highest titer compared to another sub unit protein. Various concentrations of 35.47 kDa protein (100µg, 50µg, 25µg, 12.5µg dan 6.75µg and 0µg) were used in the assay to confirm the adhesion rate into the mice enterocyte. Protein 35.75 kDa has a closer relationship with the number of bacterial adhesion. The protein concentration significantly influences the bacterial adhesion number into the mice enterocyte {(R²) 0.85, p= (<0.01) < α (0.05)}. The higher concentration of protein results on the fewer bacterial adhesions. Based on the result, it can be concluded that the sub unit protein 35.47 kDa in OMP of S.dysenteriae acts as an adhesion molecule that can inhibit the bacterial adhesion into the mice enterocyte.