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Expression of glyceraldehyde-3-phosphate dehydrogenase on the surface of Clostridium perfringens cells

Nozomu Matsunaga1, Haruka Shimizu1, Kanako Fujimoto1

  • 1Department of Life Science, Faculty of Science, Okayama University of Science, 1-1 Ridai-cho, Kita-ku, Okayama-shi, Okayama 700-0005, Japan.

Anaerobe
|May 13, 2018
PubMed

Insights

Clostridium perfringens glyceraldehyde-3-phosphate dehydrogenase (GAPDH) binds fibronectin and plasminogen. Autolysin mediates GAPDH cell surface expression, suggesting a dual role for this glycolytic enzyme.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Clostridium perfringens is a pathogenic bacterium.
  • Identifying surface proteins is crucial for understanding bacterial pathogenesis.
  • Fibronectin-binding proteins (FbPs) on bacterial surfaces mediate host-pathogen interactions.

Purpose of the Study:

  • To identify fibronectin-binding proteins (FbPs) on Clostridium perfringens.
  • To investigate the role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a potential FbP.
  • To elucidate the mechanism of GAPDH cell surface localization.

Main Methods:

  • Recombinant C. perfringens GAPDH (rGAPDH) production.
  • Ligand blotting and enzyme-linked immunosorbent assay (ELISA) for binding studies.
  • Flow cytometry to confirm cell surface expression.
  • Interaction studies between rGAPDH and C. perfringens autolysin (Acp).

Main Results:

  • Recombinant GAPDH (rGAPDH) from C. perfringens demonstrated binding to fibronectin and plasminogen.
  • rGAPDH did not bind to laminin or gelatin.
  • ELISA and flow cytometry confirmed GAPDH presence on the C. perfringens cell surface.
  • rGAPDH specifically binds to the catalytic domain of C. perfringens autolysin (Acp).

Conclusions:

  • Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is identified as a fibronectin-binding protein on Clostridium perfringens.
  • Autolysin (Acp) mediates the cell surface expression of GAPDH.
  • GAPDH exhibits a moonlighting function, binding both fibronectin and plasminogen.
  • These findings contribute to understanding C. perfringens virulence mechanisms.

Keywords:
Clostridium perfringensFibronectinFibronectin-binding proteinsGAPDH

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