Premium
The adherence of Eikenella corrodens to guinea pig macrophages in the absence and presence of anti‐bacterial antibodies
Author(s) -
Miki Y.,
Ebisu S.,
Okada H.
Publication year - 1987
Publication title -
journal of periodontal research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.31
H-Index - 83
eISSN - 1600-0765
pISSN - 0022-3484
DOI - 10.1111/j.1600-0765.1987.tb01599.x
Subject(s) - eikenella corrodens , antibody , microbiology and biotechnology , incubation , biology , galactosamine , pronase , galactose , bacteria , trypsin , immunology , biochemistry , enzyme , genetics
The interaction of oral bacteria with host cells may play an important role in the pathogenesis of periodontal disease. The purpose of this study was to investigate the adherence mechanism of Eikenella corrodens 1073 to guinea pig peritoneal macrophages in the absence or presence of anti‐bacterial antibodies. The first experiments were focused on the mechanism of E. corrodens adherence to macrophages in the absence of antibodies and complements. The adherence was dependent on time, bacterial concentration and pH. The adherence was inhibited by ethylendiaminetetraacetic acid and restored by adding calcium ions. Heating (100°C for 5 min) or protease (trypsin or pronase) treatment of bacterial cells abolished their capacity to adhere to macrophages. The specificity of E. corrodens adherence to macrophages was also proved using a hapten inhibition assay with saccharides. Among the sugars tested, the adherence was sensitive to N‐acetyl‐D‐galactosamine (GalNAc)‐ and D‐galactose (Gal)‐containing sugars. GalNAc was the most potent inhibitor, being 10 times greater than Gal. These results suggest that the adherence of E. corrodens to macrophages in the absence of antibodies and complements may require the interaction between bacterial cell surface lectins and GalNAc‐like receptors on the surface of macrophages. The second group of experiments was aimed at comparing the adherence mechanism of anti‐body‐nontreated E. corrodens to macrophages with that of antibody‐treated E. corrodens . The adherence of antibody‐treated E. corrodens reached a plateau after incubation for 10 min, whereas that of antibody‐nontreated E. corrodens reached a plateau after incubation for 30 min. The adherence of antibody‐nontreated E. corrodens was completly inhibited by GalNAc, whereas the adherence of antibody‐treated E. corrodens was only slightly inhibited by GalNAc. Treatment of macrophages with heat aggregated IgG before incubation with antibody‐treated E. corrodens caused an 80% decrease in adherence. These results show that E. corrodens adherence to GalNAc‐like receptors on the macrophage surface via bacterial lectin in the absence of antibodies is quite different from the mechanism of E. corrodens adherence to Fc receptors in the presence of bacterial antibodies.