Journal Article

The Putative Cytochrome b 5 Domain-Containing Protein CaDap1 Homologue Is Involved in Antifungal Drug Tolerance, Cell Wall Chitin Maintenance, and Virulence in Candida albicans

Zhang, Biao, Xu, Dayong, Zhang, Xing, Xu, Haitao, Zeng, Xin, Li, Feng, Mao, Hongchen, Wang, Manman

2024

Overview

( ), a prominent opportunistic fungal pathogen in humans, has garnered considerable attention due to its infectious properties. Herein, we have identified and characterized ( ), a homolog of found in . encodes a 183-amino acid protein with a conserved cytochrome 5-like heme-binding domain. The deletion of renders cells susceptible to caspofungin and terbinafine. deletion confers resistance to Congo Red and Calcofluor White, and sensitivity to sodium dodecyl sulfate. The deletion of 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, deletion results in the abnormal hyphal development of cells and diminishes virulence in a mouse systemic infection model. Thus, emerges as a critical regulator governing cellular responses to antifungal drugs, the synthesis of cell wall chitin, and virulence in .