Abstract
Porphyromonas gingivalis is a gram-negative anaerobic bacterial species implicated as an important pathogen in the development of adult periodontitis. Hemagglutinin may mediate the adsorption and invasion of bacteria into host cells. Furthermore, the hemagglutinin plays a role in the agglutinate and lyse erythrocytes intake of heme which is an absolute requirement for this bacterial growth. We previously cloned the gene encoding the 130-kDa hemagglutinin protein domain (130-kDa HMGD) and identified the functional motifs of agglutination of erythrocytes. Bacterial cell attachment to erythrocytes is an important initial step in the expression of hemolytic activity. In this study, we highly purified recombinant r130-kDa HMGD and prepared the specific antiserum. Further, the effect of the antibody on the hemolytic activity of P. gingivalis cells was examined. The polyclonal antibody recognized 43,49-kDa major bands in P. gingivalis cells and r130-kDa HMGD, and significantly inhibited the hemagglutinating and hemolytic activities of P. gingivalis cells. The findings suggest that the antibody may be useful in the development of the passive immunization against periodontal diseases caused by P. gingivalis infection.
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