Pathogenic potential of Tannerella forsythia enolase

Summary 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...

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Bibliographic Details
Published in:Molecular oral microbiology 2016-04, Vol.31 (2), p.189-203
Main Authors: Lee, J-Y., Jung, Y-J., Jun, H-K., Choi, B-K.
Format: Article
Language:English
Subjects:
Bacterial Proteins - metabolism
Bacteroides forsythus
Carrier Proteins - metabolism
Cell Line
Cells, Cultured
Cytokines - biosynthesis
Dentistry
Enzyme Activation
Enzyme-Linked Immunosorbent Assay
Fibroblasts - metabolism
fibronectin degradation
Gingiva - metabolism
Gram-Negative Bacterial Infections - microbiology
Humans
Inflammation Mediators - metabolism
Interleukins - biosynthesis
Interleukins - immunology
Monocytes
periodontitis
Periodontitis - metabolism
Periodontitis - microbiology
Phosphopyruvate Hydratase - genetics
Phosphopyruvate Hydratase - immunology
Phosphopyruvate Hydratase - metabolism
Plasminogen - analysis
plasminogen activation
proinflammatory cytokines
Tannerella forsythia - enzymology
Tannerella forsythia - genetics
Tannerella forsythia - pathogenicity
Treponema forsythia enolase
Tumor Necrosis Factor-alpha - biosynthesis
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Summary:Summary 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.
ISSN:2041-1006
2041-1014
DOI:10.1111/omi.12115