Clinical strains of Candida albicans express the surface antigen glyceraldehyde 3-phosphate dehydrogenase in vitro and in infected tissues.
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.
Gil
M L
ML
Departamento de Microbiología y Ecologia, Facultad de Farmacia, Universitat de València, Spain.
Villamón
E
E
Monteagudo
C
C
Gozalbo
D
D
Martínez
J P
JP
D000946:Antigens, Fungal / Q000276:immunology*; D000954:Antigens, Surface / Q000276:immunology*; D002176:Candida albicans / Q000276:immunology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000276:immunology*; D006801:Humans; D007124:Immunoenzyme Techniques
D000946:Antigens, Fungal; D000954:Antigens, Surface; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases