Comparative characterization of candidal cell surface–associated phosphoglycerate mutase (Gpm1) – fungal cell wall adsorption and host protein binding across pathogenic Candida species

M), and no detectable interaction for Epa3. Anti-Gpm1 antibodies reduced binding of human extracellular matrix proteins and high molecular weight kininogen (HMWK) to fungal cells by 20-25%. Microplate assays confirmed Gpm1 binding to HMWK and low molecular weight kininogen (LMWK), and chemical cross-linking combined with peptide competition mapped a key kininogen-binding region to aa116-136. Taken together, these findings support a conserved capacity of selected classical adhesins to serve as candidate docking partners for exogenous Gpm1 and demonstrate the ability of surface-associated Gpm1 to interact with the host contact system components across pathogenic yeasts.