The Putative Cytochrome <i>b</i>5 Domain-Containing Protein CaDap1 Homologue Is Involved in Antifungal Drug Tolerance, Cell Wall Chitin Maintenance, and Virulence in <i>Candida albicans</i>
2024
Dayong Xu | Manman Wang | Xing Zhang | Hongchen Mao | Haitao Xu | Biao Zhang | Xin Zeng | Feng Li
<i>Candida albicans</i> (<i>Ca</i>), a prominent opportunistic fungal pathogen in humans, has garnered considerable attention due to its infectious properties. Herein, we have identified and characterized <i>CaCDAP1</i> (<i>Ca orf19.1034</i>), a homolog of <i>ScDAP1</i> found in <i>Saccharomyces cerevisiae</i>. <i>CaCDAP1</i> encodes a 183-amino acid protein with a conserved cytochrome <i>b</i>5-like heme-binding domain. The deletion of <i>CaDAP1</i> renders <i>Ca</i> cells susceptible to caspofungin and terbinafine. <i>CaDAP1</i> deletion confers resistance to Congo Red and Calcofluor White, and sensitivity to sodium dodecyl sulfate. The deletion of <i>CaDAP1</i> results in a 50% reduction in chitin content within the cell wall, the downregulation of phosphorylation levels in CaMkc1, and the upregulation of phosphorylation levels in CaCek1. Notably, <i>CaDAP1</i> deletion results in the abnormal hyphal development of <i>Ca</i> cells and diminishes virulence in a mouse systemic infection model. Thus, <i>CaDAP1</i> emerges as a critical regulator governing cellular responses to antifungal drugs, the synthesis of cell wall chitin, and virulence in <i>Ca</i>.
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