Detection of immunodominant antigens of periodontopathic bacteria in human periodontal disease

Watanabe, Hisashi; Marsh, Philip; Ivanyi, L.

doi:10.1111/j.1399-302x.1989.tb00244.x

Cited by 35 publications

(23 citation statements)

References 23 publications

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“…The same sera recognized protein bands between 95 and 55 kDa and at 36 and 27 kDa from an A. actinomycetemcomitans sonicate. Human antibody reactivity has been reported for 55-, 47-and 40-kDa surface proteins of P. gingivalis (13) and for 75-, 57-, 51-, 46-, 35-and 19-kDa outer membrane proteins of P. gingivalis (40). Genco et al (16) reported reactivity of immune mouse sera with 43-^ 33-, 29-to 31-and 13-to 16-kDa antigens of fl gingivalis.…”

Section: Discussionmentioning

confidence: 99%

Host responses induced by co‐infection with Porphyromonas gingivalis and Actinobacillus actinomycetemcomitans in a murine model

Chen

Davern

Katz

et al. 1996

Oral Microbiology and Immunology

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In this study, evidence is presented that mixed infection with the periodontal pathogens Porphyromonas gingivalis and Actinobacillus actinomycetemcomitans results in a synergistic effect in their pathogenicity and in their ability to induce humoral and cellular host responses. BALB/c mice were injected subcutaneously on the back with P. gingivalis ATCC 53977, A. actinomycetemocomitans 75 or a mixture of both bacteria. Samples of blood and fluid from abscesses formed at the site of injection (first degree) or distant from the injection site were collected for microbiologic analysis. Serum and spleens were obtained for evaluation of humoral and cellular responses to P. gingivalis and A actinomycetemocomitans. Mice injected with A. actinomycetemcomitans had first-degree lesions only, whereas mice injected with P. gingivalis and A. actinomycetemcomitans had lesions at first- and second-degree sites from which both bacterial species were isolated. A serum anti-P. gingivalis response was induced in P. gingivalis-injected mice, which was higher in mice injected with P. gingivalis and A. actinomycetemcomitans. This pattern was not seen in the anti-A, actinomycetemcomitans response. Lymphoproliferative responses to phytohemagglutinin, Escherichia coli lipopolysaccharide and P. gingivalis of spleen cells from infected mice were decreased, especially following co-infection. Furthermore, co-infection of mice resulted in the greatest decrease in the number of CD5+, especially CD4+ lymphocytes.

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Section: Discussionmentioning

confidence: 99%

Host responses induced by co‐infection with Porphyromonas gingivalis and Actinobacillus actinomycetemcomitans in a murine model

Chen

Davern

Katz

et al. 1996

Oral Microbiology and Immunology

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“…Another major protein they detected at 47 kDa may correspond to the 48-or 46-kDa proteins that were found to be prominent in the present study. Watanabe et al (46) have detected a 46-kDa antigen from P. gingivalis sonicated whole-cell extracts and outer membrane proteins that reacts more frequently with sera from patients with severe periodontitis. This antigen may be equivalent to the 46-kDa protein detected in our study.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the immunodominant antigens of Porphyromonas gingivalis 381 in high‐responder patients

Boutsi

Koseki

Nishihara

et al. 1996

Oral Microbiology and Immunology

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The immunodominant antigens of Porphyromonas gingivalis 381 whole cells that reacted with sera from high-responder patients were examined in this study. Whole cells, phenol-water extracted lipopolysaccharide, and fimbriae from P. gingivalis 381 were analyzed using sera from 14 patients with adult periodontitis, rapidly progressive periodontitis or juvenile periodontitis as well as from two healthy subjects. Western blot analysis and enzyme-linked immunosorbent assay (ELISA) were performed. On Western blots, among many prominent protein bands, a smear was observed which was removed after adsorption of the sera with P. gingivalis phenol-water extracted lipopolysaccharide. Two major protein bands of 43 kDa and 41 kDa were found to be prominent even at very high dilutions of sera, the latter of which showed the same molecular weight as the fimbrilin band. These two bands were resistant to treatment by papain and trypsin. ELISA titers remained high after adsorption of the sera with P. gingivalis phenol-water extracted lipopolysaccharide. The results of this study suggest that the 43-kDa and the fimbrilin (41 kDa) proteins may play an important role as immunodominant antigens of P. gingivalis 381.

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“…Although the presence of an elevated antibody response to P. gingiualis whole cells in individuals with a history of periodontitis has been known for some time, the nature of the moieties on the surface of the organism, particularly the protein antigens, which are recognised by these antibodies has only recently become evident and a number of putative immunodominant antigens are now being identified [6][7][8][9][10][11][12][13][14][15]. We recently examined the immunoreactivity of the surface proteins of P. gingivalis W83 using sera from a case:control study of adult periodontitis [16].…”

Section: Introductionmentioning

confidence: 99%

Production and characterisation of monoclonal antibodies to the principle sonicate antigens of Porphyromonas gingivalis w50

Millar

1993

FEMS Immunology and Medical Microbiology

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Protein antigens from whole cell sonicates of Porphyromonas gingivalis W50, previously shown to be discriminatory antigens for patients with adult periodontitis, were purified using SDS-PAGE. Electroeluted proteins were used to immunize mice for the production of monoclonal antibodies (mAbs). A combination of enzyme-linked immunosorbent assay (ELISA) and Western blotting were used to screen hybridoma supernatants for mAbs. MAbs were successfully raised against M(r) 115,000, M(r) 55,000 and M(r) 47,000 antigens together with a second M(r) 55,000 polypeptide which was a contaminant of the M(r) 55,000 antigen. No immunological cross-reactivity was found between these four proteins. The mAbs were used to examine the distribution of these antigens among fifteen P. gingivalis strains together with related oral bacteria using immunostaining of dot blots and Western blots. The antigens were confined to P. gingivalis with the M(r) 115,000 and M(r) 47,000 antigens being present in all strains tested. The distribution of the M(r) 55,000 antigens were slightly more restricted: one M(r) 55,000 (outer membrane location) was present in nine of the fifteen P. gingivalis strains tested, while the other M(r) 55,000 (location unknown) was only absent from one strain. Whole cell ELISA demonstrated that the M(r) 115,000 and the outer membrane M(r) 55,000 antigen possess epitopes which are located on the surface of the bacterium.

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Detection of immunodominant antigens of periodontopathic bacteria in human periodontal disease

Cited by 35 publications

References 23 publications

Host responses induced by co‐infection with Porphyromonas gingivalis and Actinobacillus actinomycetemcomitans in a murine model

Host responses induced by co‐infection with Porphyromonas gingivalis and Actinobacillus actinomycetemcomitans in a murine model

Characterization of the immunodominant antigens of Porphyromonas gingivalis 381 in high‐responder patients

Production and characterisation of monoclonal antibodies to the principle sonicate antigens of Porphyromonas gingivalis w50

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