The GPI-Anchored Aspartyl Proteases Encoded by the YPS1 and YPS7 Genes of Candidozyma auris and Their Role Under Stress Conditions

<i>Candidozyma auris</i> is a multidrug-resistant, thermo- and osmotolerant yeast capable of persisting on biotic and abiotic surfaces, attributes likely linked to its cell wall composition. Here, seven putative genes encoding yapsins, aspartyl proteases GPI-anchored to the membrane or cell wall, were identified in the genomes of <i>C. auris</i> CJ97 and 20-1498, from clades III and IV, respectively. The <i>C. auris YPS1</i> gene is orthologous to the <i>SAP9</i> of <i>C. albicans</i>. The <i>YPS7</i> gene is orthologous to <i>YPS7</i> in <i>C. glabrata</i> and <i>S. cerevisiae</i>, so that they may share similar roles. An in silico analysis suggested an interaction between pepstatin and the catalytic domain of Yps1 and Yps7. Although this inhibitor, when combined with caffeine, had a subtle effect on the growth of <i>C. auris</i>, it induced alterations in the cell wall. <i>CauYPS1</i> and <i>CauYPS7</i> expression increased under nutrient starvation and NaCl, and at 42 °C. The transcriptome of the 20-1498 strain suggests that autophagy may play a role in thermal stress, probably degrading deleterious proteins or maintaining cell wall and vacuolar homeostasis. Therefore, CauYps1 and CauYps7 may play a role in the cell wall integrity of <i>C. auris</i> in stress conditions, and they could be a target of new antifungal or antivirulence agents.