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- W2156810094 abstract "By immunoelectron microscopy with a polyclonal antibody against the cytosolic glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Candida albicans (anti-GAPDH PAb), the protein was clearly detected at the outer surface of the cell wall, particularly on blastoconidia, as well as in the cytoplasm. Intact blastoconidia were able to adhere to fibronectin and laminin immobilized on microtiter plates, and this adhesion was markedly reduced by both the anti-GAPDH PAb and soluble GAPDH from Saccharomyces cerevisiae. In addition, semiquantitative flow cytometry analysis with the anti-GAPDH PAb showed a decrease in antibody binding to cells in the presence of soluble fibronectin and laminin. Purified cytosolic C. albicans GAPDH was found to bind to fibronectin and laminin in a ligand Western blot assay. These observations suggest that the cell wall-associated form of the GAPDH in C. albicans could be involved in mediating adhesion of fungal cells to fibronectin and laminin, thus contributing to the attachment of the microorganism to host tissues and to the dissemination of Candida infection." @default.
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- W2156810094 date "1998-05-01" @default.
- W2156810094 modified "2023-10-18" @default.
- W2156810094 title "The Cell Wall-Associated Glyceraldehyde-3-Phosphate Dehydrogenase of <i>Candida albicans</i> Is Also a Fibronectin and Laminin Binding Protein" @default.
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- W2156810094 doi "https://doi.org/10.1128/iai.66.5.2052-2059.1998" @default.
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