Role of Porphyromonas gingivalis 40-kDa outer membrane protein in the aggregation of P. gingivalis vesicles and Actinomyces viscosus

Hiratsuka, Koichi; Abiko, Yoshimitsu; Hayakawa, Mitsuo; Itô, Teiichiro; Sasahara, Hiroshige; Takiguchi, Hisashi

doi:10.1016/0003-9969(92)90078-m

Cited by 76 publications

(64 citation statements)

References 34 publications

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“…Its fimbriae have been shown to interact with epithelial cells (15), cultured human fibroblasts (20), and saliva-coated hydroxyapatite beads (2,32), while its vesicles have been shown to interact with collagen-coated hydroxyapatite beads (32). Further, in studies to determine which of the surface components of P. gingivalis interact with grampositive bacteria, its fimbriae have been reported to interact with A. viscosus (12) and S. gordonii (24); its vesicles have been reported to interact with A. naeslundii (8), A. viscosus (13), and S. mutans (17); and its hemagglutinin has been reported to interact with A. viscosus (34).…”

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confidence: 99%

Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus oralis Functions as a Coadhesin for Porphyromonas gingivalis Major Fimbriae

et al. 2004

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Cohesive interactions between Porphyromonas gingivalis and plaque-forming bacteria, such as Streptococcus oralis, are considered to play an important role in the colonization of P. gingivalis in periodontal sites. Although P. gingivalis fimbriae have been reported to mediate coaggregation with S. oralis, the S. oralis molecule involved has not been identified. We identified the coadhesin of S. oralis ATCC 9811 and purified it by affinity column chromatography. We found that the molecular mass of the purified protein was approximately 40 kDa. Dot blot and Western blot assays showed binding of the 40-kDa protein to P. gingivalis fimbriae. Further, turbidimetric assays showed that the coadhesin inhibited coaggregation between P. gingivalis and S. oralis in a dose-dependent manner. Analyses of the amino-terminal sequences of the protein and its lysyl endopeptidase-cleaved fragments revealed that the coadhesin was identical to glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Next, we cloned the gene that encodes S. oralis GAPDH and found that the sequence had a high degree of homology with the sequences of GAPDHs of various bacteria, including Streptococcus gordonii and Fusobacterium nucleatum. To confirm the contribution of S. oralis GAPDH to the interaction with P. gingivalis, a recombinant GAPDH protein was generated in Escherichia coli; this protein bound to P. gingivalis fimbriae and had an inhibitory effect on coaggregation. These results suggest that S. oralis GAPDH functions as a coadhesin for P. gingivalis fimbriae. In addition, considering the high degree of homology of the GAPDHs of various bacteria, those of other plaque-forming bacteria also may contribute to the colonization of P. gingivalis.Porphyromonas gingivalis is considered to be a prominent periodontopathogen, as it possesses a variety of virulence factors, such as proteinases, hemagglutinin, and lipopolysaccharide (28,37,41). In order to cause infection, it is necessary for P. gingivalis to attach to tooth surfaces, subgingival epithelium, or early colonizing gram-positive bacteria; this step constitutes the initial stage of colonization in periodontal pockets (38). In addition, the bacterium has been reported to interact with a variety of other oral gram-positive bacteria (19), including Actinomyces naeslundii (36, 43), Actinomyces viscosus (9, 12, 26, 27, 36), Streptococcus gordonii (23), Streptococcus mutans (17), Streptococcus oralis (29), and Streptococcus sanguis (39); these interactions are considered to play a vital role in the colonization of P. gingivalis in the oral cavity.P. gingivalis possesses several cell surface components that are important for its attachment. Its fimbriae have been shown to interact with epithelial cells (15), cultured human fibroblasts (20), and saliva-coated hydroxyapatite beads (2, 32), while its vesicles have been shown to interact with collagen-coated hydroxyapatite beads (32). Further, in studies to determine which of the surface components of P. gingivalis interact with grampositive bacteria, its fimbri...

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Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus oralis Functions as a Coadhesin for Porphyromonas gingivalis Major Fimbriae

et al. 2004

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“…40k-OMP is a highly immunogenic surface protein of P. gingivalis, which has been receiving attention as a periodontal disease vaccine. In this regard, it has been shown that 40k-OMP-specific rabbit monoclonal antibodies inhibit coaggregation activity of P. gingivalis (14,16,20). Further, these monoclonal antibodies possess complement-mediated bactericidal activity to P. gingivalis (17,18).…”

Section: Discussionmentioning

confidence: 99%

“…viscosus (14,16). Further, these monoclonal antibodies possess a complement-mediated bactericidal activity to P gingivalis (17,18).…”

Section: Introductionmentioning

confidence: 98%

Nasal Immunization with P. gingivalis Surface Protein Antigen and Cholera Toxin Adjuvant Induces T Helper 2 Responses in Both Mucosal and Systemic Compartments

et al. 2003

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It is well establishedthat Porphyromonas gingivalisis one of the major pathogens of adult periodontitis. P. gingivalis produces an outer membrane protein with a molecular mass of 40-kDa (40k-OMP). In the present study, in order to assess the potential for application of 40k-OMP in the development of an antiperiodontal disease vaccine, we analyzed 40k-OMP-specific CD4+ T helper (Th) cell responses induced in the mucosal as well as systemic compartments when 40k-OMP was administered nasally. When CD4+T cells that were isolated from cervical lymph nodes (CLN) and spleens of mice immunized with 40k-OMP plus cholera toxin (CT) as adjuvant were re-stimulated with 40k-OMP in vitro, significant levels of proliferative responses were induced. In contrast, essentially no increased proliferation occurred in CLN and spleens taken from mice given 40k-OMP alone. Analysis of T helper (Th) 1 (IFN-y) and Th2 (IL-4, IL-5 and IL-6) cytokine responses showed that 40k-OMP-specific Th cells from both CLN and the spleen produced significant levels of IL-4, IL-5 and IL-6 but did not result in changes in IFN-y production. In contrast, marginal levels of IL-4, IL-5 and IL-6 production were seen in mice given 40k-OMP alone nasally. These results suggest that nasal administration of 40k-OMP plus CT as an adjuvant can elicit 40k-OMP-specific Th2-type cytokine responses in both mucosal and systemic compartments. Further, the nasal 40k-OMP vaccine possesses the potential for antiperiodontal vaccine.

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“…Since the affinity-purified rabbit polyclonal antibody (Af-PAb) against the recombinant protein significantly inhibits aggregation activity ofP gingivalis vesicles to oral Gram-positive bacteria, the 40-kDa OMP may be an important aggregation factor off! gingivalis (6). Since 40-kDa OMP gene probe hybridized with all P gingivalis strains tested including clinical isolates, the 40-kDa OMP is conserved in P. gingivalis species (7).…”

Section: Introductionmentioning

confidence: 99%

Identification of the functional domain in a coaggregation factor from Porphyromonas gingivalis

et al. 2003

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Porphyromonas gingivalis has been implicated as a major pathogen in periodontal diseases. The coaggregation factor plays an important role in colonization of P. gingivalis in the subgingival area through aggregation with other extantoral microorganisms. We previouslysucceededin gene cloning of the 40-kDa outer membrane protein (OMP) from P gingivalis and identified the 40-kDa OMP as one of coaggregation factors. The mouse monoclonal antibodyPg-omp-A2, which inhibitedthe coaggregationactivityof P gingivalis, was successfullyconstructed. In order to develop a useful immunotherapy, it is essential to understand the functional domain expressing aggregation activity. The availability of recombinant 40-kDa OMP and the identification of the antigenic determinant recognized by Pg-omp-A2 willallowfor thedetermination of the functional domain of the coaggregation factor.In this study,we used a phage-displayed epitope mapping system to examine the functional domain expressing aggregation activity. Peptide-displayed phage clones were isolated by biopanning using Pg-omp-A2 and determined DNA nucleotide sequence and then predicted the amino acid sequence of epitope. The amino acid sequence of epitope region was similar to the region of %IALDQTLGIP105 in 40-kDa OMP. Next, a series of 6 peptides (designated peptideA to F) in 40-kDa OMP was designed and chemically synthesized, and then we examined their immuno-reactivity by Pg-omp-A2. Pg-omp-A2 recognizedthe peptide C that contained the IALDQTLGEP amino acid sequence. Furthermore, the peptide C reduced the inhibitory activity of Pg-omp-A2 against the aggregation of P. gingivalis vesicles with Streptococcus gordonii. These findings suggest that the aggregation-associated domain of P gingivalis 40-kDa coaggregation factor may be IALDQTLGIP.

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Role of Porphyromonas gingivalis 40-kDa outer membrane protein in the aggregation of P. gingivalis vesicles and Actinomyces viscosus

Cited by 76 publications

References 34 publications

Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus oralis Functions as a Coadhesin for Porphyromonas gingivalis Major Fimbriae

Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus oralis Functions as a Coadhesin for Porphyromonas gingivalis Major Fimbriae

Nasal Immunization with P. gingivalis Surface Protein Antigen and Cholera Toxin Adjuvant Induces T Helper 2 Responses in Both Mucosal and Systemic Compartments

Identification of the functional domain in a coaggregation factor from Porphyromonas gingivalis

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