title: Pathogenic potential of Tannerella forsythia enolase.
abstract: Although enolases are cytosolic enzymes involved in the glycolytic pathway, they can also be secreted or expressed on the surface of a variety of eukaryotic cells and bacteria. Surface-exposed enolases of eukaryotes and bacteria can function as plasminogen receptors. Furthermore, antibodies raised against bacterial enolases can react with host enolases, suggesting molecular mimicry between bacterial and host enzymes. In this study, we analyzed an enolase of the major periodontopathogen Tannerella forsythia, which is either secreted or present on the cell surface, via matrix-assisted laser desorption ionization time-of-flight mass spectrometry and immunofluorescence, respectively. The T. forsythia enolase retained the enzymatic activity converting 2-phosphoglycerate to phosphoenolpyruvate and showed plasminogen binding and activating ability, which resulted in the degradation of fibronectin secreted from human gingival fibroblasts. In addition, it induced proinflammatory cytokine production, including interleukin-1β (IL-1β), IL-6, IL-8, and tumour necrosis factor-α (TNF-a) in the human THP-1 monocytic cell line. Taken together, our results demonstrate that T. forsythia enolase plays a role in pathogenesis in the host by plasminogen activation and proinflammatory cytokine induction, which has the potential to exaggerate inflammation in periodontitis.
authors.affiliation: Department of Oral Microbiology and Immunology, School of Dentistry, Seoul National University, Seoul, Korea.
authors.forename: J-Y
authors.initials: JY
authors.lastname: Lee
authors.affiliation: Department of Oral Microbiology and Immunology, School of Dentistry, Seoul National University, Seoul, Korea.
authors.forename: Y-J
authors.initials: YJ
authors.lastname: Jung
authors.affiliation: Department of Oral Microbiology and Immunology, School of Dentistry, Seoul National University, Seoul, Korea.
authors.forename: H-K
authors.initials: HK
authors.lastname: Jun
authors.affiliation: Department of Oral Microbiology and Immunology, School of Dentistry, Seoul National University, Seoul, Korea.|Dental Research Institute, Seoul National University, Seoul, Korea.
authors.forename: B-K
authors.initials: BK
authors.lastname: Choi
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D002352:Carrier Proteins / Q000378:metabolism; D002460:Cell Line; D002478:Cells, Cultured; D016207:Cytokines / Q000096:biosynthesis; D004789:Enzyme Activation; D004797:Enzyme-Linked Immunosorbent Assay; D005347:Fibroblasts / Q000378:metabolism; D005881:Gingiva / Q000378:metabolism; D016905:Gram-Negative Bacterial Infections / Q000382:microbiology; D006801:Humans; D018836:Inflammation Mediators / Q000378:metabolism; D007378:Interleukins / Q000096:biosynthesis / Q000276:immunology; D009000:Monocytes; D010518:Periodontitis / Q000378:metabolism / Q000382:microbiology; D010751:Phosphopyruvate Hydratase / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D010958:Plasminogen / Q000032:analysis; D000070436:Tannerella forsythia / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity*; D014409:Tumor Necrosis Factor-alpha / Q000096:biosynthesis
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D016207:Cytokines; D018836:Inflammation Mediators; D007378:Interleukins; C439524:TNF protein, human; D014409:Tumor Necrosis Factor-alpha; D010958:Plasminogen; D010751:Phosphopyruvate Hydratase
keywords: Treponema forsythia enolase; fibronectin degradation; periodontitis; plasminogen activation; proinflammatory cytokines