Binding of Complement Inhibitor C4b-Binding Protein Contributes to Serum Resistance of <i>Porphyromonas gingivalis</i>

DOI PDF 被引用文献7件
  • Michal Potempa
    Department of Laboratory Medicine, Section of Medical Protein Chemistry, University Hospital Malmö, Lund University , Malmö,
  • Jan Potempa
    Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University , Krakow,
  • Marcin Okroj
    Department of Laboratory Medicine, Section of Medical Protein Chemistry, University Hospital Malmö, Lund University , Malmö,
  • Katarzyna Popadiak
    Department of Laboratory Medicine, Section of Medical Protein Chemistry, University Hospital Malmö, Lund University , Malmö,
  • Sigrun Eick
    Department of Medical Microbiology, University Hospital of Jena , Jena,
  • Ky-Anh Nguyen
    Westmead Centre for Oral Health, Institute of Dental Research , Sydney,
  • Kristian Riesbeck
    Department of Laboratory Medicine, Section of Medical Microbiology, University Hospital Malmö, Lund University , Malmö,
  • Anna M Blom
    Department of Laboratory Medicine, Section of Medical Protein Chemistry, University Hospital Malmö, Lund University , Malmö,

書誌事項

公開日
2008-10
権利情報
  • https://academic.oup.com/pages/standard-publication-reuse-rights
DOI
  • 10.4049/jimmunol.181.8.5537
公開者
Oxford University Press (OUP)

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<jats:title>Abstract</jats:title> <jats:p>The periodontal pathogen Porphyromonas gingivalis is highly resistant to the bactericidal activity of human complement, which is present in the gingival crevicular fluid at 70% of serum concentration. All thirteen clinical and laboratory P. gingivalis strains tested were able to capture the human complement inhibitor C4b-binding protein (C4BP), which may contribute to their serum resistance. Accordingly, in serum deficient of C4BP, it was found that significantly more terminal complement component C9 was deposited on P. gingivalis. Moreover, using purified proteins and various isogenic mutants, we found that the cysteine protease high molecular weight arginine-gingipain A (HRgpA) is a crucial C4BP ligand on the bacterial surface. Binding of C4BP to P. gingivalis appears to be localized to two binding sites: on the complement control protein 1 domain and complement control protein 6 and 7 domains of the α-chains. Furthermore, the bacterial binding of C4BP was found to increase with time of culture and a particularly strong binding was observed for large aggregates of bacteria that formed during culture on solid blood agar medium. Taken together, gingipains appear to be a very significant virulence factor not only destroying complement due to proteolytic degradation as we have shown previously, but was also inhibiting complement activation due to their ability to bind the complement inhibitor C4BP.</jats:p>

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