Abstract
Streptococcus intermedius is a causative agent of brain or liver abscesses. S. intermedius produces intermedilysin that plays a pivotal role in pathogenicity. We identified other pathogenic factors and described a fibronectin binding protein (FBP) homolog of S. intermedius (FbpI) that mediated bacterial adhesion to epithelial cells and virulence for mice. The amino acid sequence of FbpI is similar to that of atypical FBPs, which do not possess a conventional secretion signal and an anchoring motif. A full-length recombinant FbpI (rFbpI) bound to immobilized fibronectin in a dose-dependent manner. The fibronectin binding activity of an N-terminal construct of rFbpI comprising the translation initiation methionine of the open reading frame to lysine 265 (rFbpI-N) bound immobilized fibronectin to a much lesser extent compared with rFbpI. A construct comprising the C-terminal domain (alanine 266 to methionine 549; rFbpI-C) bound immobilized fibronectin equivalently to rFbpI. Adherence of the isogenic mutant ΔfbpI to cultured epithelial cells and immobilized fibronectin was significantly lower than that of the wild-type strain. Abscess formation of ΔfbpI reduced in a mouse infection model compared with that in the wild-type. Thus, FbpI may play a role in bacterial adhesion to host cells and represent a critical pathogenic factor of S. intermedius.
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Acknowledgements
We thank Dr. Nakano at Okayama University, Okayama, Japan and Dr. Ooshima at Kansai Women’s College, Osaka Japan, for kindly providing the antigen I/II antiserum of S. mutans. This work was supported, in part, by a Grant-in-Aid for Scientific Research (17K11623 and 17K17286) from the Ministry of Education, Culture, Sports, Science and Technology, Japan.
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Kodama, Y., Shimoyama, Y., Ishikawa, T. et al. Characterization and pathogenicity of fibronectin binding protein FbpI of Streptococcus intermedius. Arch Microbiol 202, 2071–2081 (2020). https://doi.org/10.1007/s00203-020-01922-y
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DOI: https://doi.org/10.1007/s00203-020-01922-y