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Protein-related hydrophobicity differences among strains belonging to Candidozyma auris (Candida auris) clades
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DOI：10.1128/spectrum.02897-25.png)
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Abstract
En 中文
In recent years, Candidozyma auris (Candida auris) has emerged as a threat to human health due to its combination of virulence and antifungal resistance. This fungal pathogen is notable for its thermotolerance and a strong attachment capability that confers environmental persistence and immune evasion. Here, we compared strains from five clades of C. auris: clade I = South Asia (CDC 387), clade II = East Asia (CDC 381), clade III = Africa (CDC 384), clade IV = South America (CDC 385), and clade V = Iran (CDC 1097) for their ability to regulate cell surface hydrophobicity and biofilm. The hydrophobicity varied for each C. auris clade, with strains 384, 385, and 1097 displaying the highest hydrophobicity levels. C. auris strains had variable biofilm levels when compared among clades and had lower or similar biofilm levels when compared with Candida albicans at different temperatures. Comparison of mass spectrometry analysis of proteolytic digestates of cells from strains with low or high hydrophobicity revealed putative surface hydrophobic proteins. These included homologs to Candida albicans Als3 and IFF proteins, and their contribution to hydrophobicity and biofilm formation was confirmed with gene-deficient (knockout) C. auris strains. We conclude that several proteins contribute to C. auris surface hydrophobicity.IMPORTANCECandidozyma auris (Candida auris) is an emerging pathogenic microorganism that is rapidly gaining attention due to outbreaks in health care facilities and its multidrug resistance. Its origin has yet to be determined, but genotypic analyses have pointed toward a simultaneous independent emergence of the different clades, possibly implicating climate change as a major factor in its recent appearance as a fungal pathogen. In 2022, the World Health Organization placed C. auris in the critical priority group as the second greatest fungal threat globally. Due to limited immunological and proteomic studies of C. auris, we sought to elucidate possible virulence mechanisms and identify leading proteins that can be targeted by immunotherapies and new drugs. Using proteomic analysis, we identified 12 lead proteins related to C. auris hydrophobicity and adhesion, implying that these properties are conferred by multiple proteins.
Keywords:
C. auris
hydrophobicity
proteins
mass spectrometry
biofilms
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