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

Nozomu Matsunaga, Haruka Shimizu, Kanako Fujimoto, Kanako Watanabe, Tsutomu Yamasaki, Naoya Hatano, Eiji Tamai, Seiichi Katayama, Yasuo Hitsumoto

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

During research to identify fibronectin (Fn)-binding proteins (Fbps) on the surface of Clostridium perfringens cells, we identified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a candidate Fbp. GAPDH is a glycolytic enzyme found in a wide range of prokaryotes and eukaryotes. The Fn-binding activity of recombinant C. perfringens GAPDH (rGAPDH) was investigated using both ligand blotting analysis and enzyme-linked immunosorbent assay (ELISA). rGAPDH strongly bound plasminogen but not laminin or gelatin. Although GAPDH has no signal sequence, it is expressed on the cell surface of many microorganisms. The presence of GAPDH on the surface of C. perfringens cells was analyzed using ELISA and flow cytometry analyses; purified rGAPDH bound to the surface of C. perfringens cells. As autolysin is reportedly involved in the binding of GAPDH to the cell surface, we evaluated the interaction between rGAPDH and the C. perfringens autolysin Acp by both ELISA and ligand blotting assay. These assays revealed that rGAPDH binds to the catalytic domain of Acp but not the cell wall binding domains. These results suggest that autolysin mediates expression of GAPDH on the surface of C. perfringens cells and indicate a possible moonlighting function for GAPDH in binding both Fn and plasminogen.

Original languageEnglish
Pages (from-to)124-130
Number of pages7
JournalAnaerobe
Volume51
DOIs
Publication statusPublished - Jun 2018
Externally publishedYes

Keywords

  • Clostridium perfringens
  • Fibronectin
  • Fibronectin-binding proteins
  • GAPDH

ASJC Scopus subject areas

  • Microbiology
  • Infectious Diseases

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