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Infect Immun. 1989 February; 57(2): 566-573

Immunochemical identification and preliminary characterization of a nonfimbrial hemagglutinating adhesin of Bacteroides gingivalis.

Ecole de Médecine Dentaire, Université Laval, Québec, Canada.

ABSTRACT

A cell-bound hemagglutinating adhesin (HA-Ag2) of Bacteroides gingivalis was identified by crossed immunoaffinity electrophoresis as one of the common antigens of the species. A polyclonal antiserum with a restricted specificity for HA-Ag2 was produced by immunizing with the relevant immunoprecipitate excised from crossed-immunoelectrophoresis gels. The immunoglobulin G fraction of this monospecific antiserum inhibited hemagglutination. The antiserum was used against a cell surface extract of B. gingivalis in immunoblotting experiments, and we detected two antigens with apparent molecular masses of 33 and 38 kilodaltons in B. gingivalis ATCC 33277 and W83. Monoclonal antibody, C1.17, produced in another laboratory against B. gingivalis 381 and characterized as showing reactivity with a hemagglutinin of this strain (Y. Naito, K. Okuda, T. Kato, and I. Takazoe, Infect. Immun. 50:231-235, 1985), was also used to produce immunoblots of extracts of strains ATCC 33277 and W83. The apparent molecular masses of the major polypeptides recognized by monoclonal C1.17 in the immunoblots were the same as those detected by the polyclonal monospecific antiserum, i.e., 33 and 38 kilodaltons. Significantly, none of the polypeptides identified in this study corresponded to the polypeptide appearing in the 41- to 43-kilodalton region and identified by Yoshimura and co-workers (F. Yoshimura, K. Takahashi, N. Yoshinobu, and T. Suzuki, J. Bacteriol. 160:949-957, 1984) as the fimbrial protein characteristic of the species. Enzyme-linked immunosorbent assay inhibition experiments with the monospecific antiserum indicated that the cell surface extracts from strains ATCC 33277 and W83 were strong inhibitors, whereas the fimbria-enriched preparations from both strains failed to inhibit binding of antibodies to the cell surface antigens. As a whole, our study indicates that a nonfimbrial surface protein complex demonstrating erythrocyte-binding capacity, HA-Ag2, is common to three strains of B. gingivalis and is composed of at least two associated polypeptides with apparent molecular masses of 33 and 38 kilodaltons which share at least one antigenic determinant.

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