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Background  Triosephosphate isomerase (Tpi1) is a glycolytic enzyme that has recently been reported also to be an atypical proteinaceous component of the  Candida  yeast cell wall. Similar to other known candidal “moonlighting proteins”, surface-exposed Tpi1 is likely to contribute to fungal adhesion during the colonization and infection of a human host. The aim of our present study was to directly prove the presence of Tpi1 on  C. albicans  and  C. glabrata  cells under various growth conditions and characterize the interactions of native Tpi1, isolated and purified from the candidal cell wall, with human extracellular matrix proteins.    Results  Surface plasmon resonance measurements were used to determine the dissociation constants for the complexes of Tpi1 with host proteins and these values were found to fall within a relatively narrow range of 10 − 8 -10 − 7  M. Using a chemical cross-linking method, two motifs of the Tpi1 molecule (aa 4–17 and aa 224–247) were identified to be directly involved in the interaction with vitronectin. A proposed structural model for Tpi1 confirmed that these interaction sites were at a considerable distance from the catalytic active site. Synthetic peptides with these sequences significantly inhibited Tpi1 binding to several extracellular matrix proteins suggesting that a common region on the surface of Tpi1 molecule is involved in the interactions with the host proteins.    Conclusions  The current study provided structural insights into the interactions of human extracellular matrix proteins with Tpi1 that can occur at the cell surface of  Candida  yeasts and contribute to the host infection by these fungal pathogens.    Supplementary Information  The online version contains supplementary material available at 10.1186/s12866-021-02235-w.

bmc microbiology

Candida albicans and Candida glabrata triosephosphate isomerase – a moonlighting protein that can be exposed on the candidal cell surface and bind to human extracellular matrix proteins