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

DOI Web Site 参考文献17件
  • Yamada Kazuaki
    Department of Biochemistry, Nihon University School of Dentistry at Matsudo
  • Shibata Yasuko
    Department of Biochemistry, Nihon University School of Dentistry at Matsudo Research Institute of Oral Science, Nihon University School of Dentistry at Matsudo
  • Kiyama-Kishikawa Michiko
    Department of Biochemistry, Nihon University School of Dentistry at Matsudo Research Institute of Oral Science, Nihon University School of Dentistry at Matsudo
  • Abiko Yoshimitsu
    Department of Biochemistry, Nihon University School of Dentistry at Matsudo Research Institute of Oral Science, Nihon University School of Dentistry at Matsudo

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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 extant oral microorganisms. We previously succeeded in 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 antibody Pg-omp-A2, which inhibited the coaggregation activity of P gingivalis, was successfully constructed. 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 will allow for the determination of the functional domain of the coaggregation factor.<br>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 96IALDQTLGIP105 in 40-kDa OMP. Next, a series of 6 peptides (designated peptide A 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 recognized the peptide C that contained the IALDQTLGIP 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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  • ＩＪＯＭＳ

    ＩＪＯＭＳ 1 (2), 97-102, 2003

    日本大学松戸歯学部 口腔科学研究所

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