Clinical Strains of Candida Albicans Express the Surface Antigen Glyceraldehyde 3-phosphate Dehydrogenase in Vitro and in Infected Tissues

FEMS Immunol Med Microbiol. 1999 Mar;23(3):229-34. doi: 10.1111/j.1574-695X.1999.tb01243.x.

Abstract

We have previously described the presence of an enzymatically active form of glyceraldehyde 3-phosphate-dehydrogenase (GAPDH) in the cell surface of Candida albicans ATCC 26555 which is also a fibronectin and laminin binding protein. Immunohistochemical analysis of tissue sections from patients with disseminated candidiasis with a polyclonal antiserum to GAPDH from C. albicans (PAb anti-CA-GAPDH) revealed that the enzyme is expressed at the surface of fungal cells in infected tissues. The same PAb detected the presence of GAPDH species, with a molecular mass of approximately 33 kDa, in cell wall extracts obtained from clinical isolates of the fungus. These cell surface-bound GAPDH moieties exhibited a dose-dependent dehydrogenase activity. These results indicate that this cell surface-bound GAPDH plays a role during infection probably contributing to the attachment of fungal cells to host tissues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Fungal / immunology*
  • Antigens, Surface / immunology*
  • Candida albicans / immunology*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / immunology*
  • Humans
  • Immunoenzyme Techniques

Substances

  • Antigens, Fungal
  • Antigens, Surface
  • Glyceraldehyde-3-Phosphate Dehydrogenases