Open AccessClinical strains of Candida albicans express the surface antigen glyceraldehyde 3‐phosphate dehydrogenase in vitro and in infected tissues
Author(s) -
Gil M.Luisa,
Villamón Eva,
Monteagudo Carlos,
Gozalbo Daniel,
Martínez José P.
Publication year - 1999
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.1999.tb01243.x
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , biology , candida albicans , dehydrogenase , polyclonal antibodies , antigenicity , microbiology and biotechnology , antiserum , glyceraldehyde , antigen , lysis , enzyme , biochemistry , immunology
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.