title: Hemin-binding protein 35 (HBP35) plays an important role in bacteria-mammalian cells interactions in Porphyromonas gingivalis.
abstract: Hemin-binding protein 35 (HBP35) may be an essential protein for bacterial survival in evasion from environmental stress in Porphyromonas gingivalis. The anti-recombinant HBP35 antibody inhibits P. gingivalis hemagglutination. This study considered the role of this protein for hemagglutination and adherence to host cells using the HBP35-deficient mutant (MD774) derived from P. gingivalis FDC381. FDC381 had strong hemagglutination activity, whereas MD774 had no activity. Anti-130-kDa hemagglutinin antibody, mAb-Pg-vc, reacted mainly with the 43- and 49-kDa molecules in the membrane fraction. However, no proteins reacted in the MD774. The hemolytic activity in MD774 was much lower than that in FDC381. Anti-recombinant HBP35 antibody strongly inhibited the P. gingivalis FDC381 adherence to epithelial cells. In addition, MD774 exhibited a significant decrease in the adherence. The hydrophobicity of MD774 was equal to 19.4% of that of FDC381. SDS-PAGE profiling of the membrane fractions of both strains showed very different profiles. Taken together, these findings suggest that HBP35 plays a role, not only in hemin-binding, but also in multiple P. gingivalis binding to erythrocytes, and host epithelial gingival cells. In addition, this protein may directly and/or indirectly affect the virulence of this organism.
authors.affiliation: Department of Biochemistry and Molecular Biology, Nihon University School of Dentistry at Matsudo, Matsudo, Chiba 271-8587, Japan. hiratsuka.koichi@nihon-u.ac.jp <hiratsuka.koichi@nihon-u.ac.jp>
authors.forename: Koichi
authors.initials: K
authors.lastname: Hiratsuka
authors.forename: Michiko
authors.initials: M
authors.lastname: Kiyama-Kishikawa
authors.forename: Yoshimitsu
authors.initials: Y
authors.lastname: Abiko
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000907:Antibodies, Bacterial / Q000276:immunology; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000502:physiology*; D002352:Carrier Proteins / Q000037:antagonists & inhibitors / Q000502:physiology*; D002460:Cell Line; D002462:Cell Membrane / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D004847:Epithelial Cells / Q000382:microbiology; D004912:Erythrocytes / Q000382:microbiology*; D017353:Gene Deletion; D006384:Hemagglutination; D000081062:Heme-Binding Proteins; D006420:Hemeproteins / Q000037:antagonists & inhibitors / Q000172:deficiency / Q000502:physiology*; D006461:Hemolysis; D054884:Host-Pathogen Interactions; D006801:Humans; D008969:Molecular Sequence Data; D016966:Porphyromonas gingivalis / Q000472:pathogenicity*; D020543:Proteome / Q000032:analysis; D012756:Sheep; D037521:Virulence Factors / Q000037:antagonists & inhibitors / Q000172:deficiency / Q000502:physiology*
chemical_list: D000907:Antibodies, Bacterial; D001426:Bacterial Proteins; D002352:Carrier Proteins; D000081062:Heme-Binding Proteins; D006420:Hemeproteins; D020543:Proteome; D037521:Virulence Factors