AI Article Synopsis
- Antifungal resistance is a growing global problem, highlighting the need for new treatment options.
- CBS is identified as a key enzyme in producing hydrogen sulfide in pathogenic fungi, and its deletion negatively impacts fungal growth and virulence.
- Protolichesterinic acid, derived from lichen, has been found to inhibit CBS, reducing fungal virulence and showing promise in treating infections in mouse models.
Article Abstract
The global emergence of antifungal resistance threatens the limited arsenal of available treatments and emphasizes the urgent need for alternative antifungal agents. Targeting fungal pathogenic functions is an appealing alternative therapeutic strategy. Here, we show that cystathionine β-synthase (CBS), compared with cystathionine γ-lyase, is the major enzyme that synthesizes hydrogen sulfide in the pathogenic fungus . Deletion of CBS leads to deficiencies in resistance to oxidative stress, retarded cell growth, defective hyphal growth, and increased β-glucan exposure, which, together, reduce the pathogenicity of . By high-throughput screening, we identified protolichesterinic acid, a natural molecule obtained from a lichen, as an inhibitor of CBS that neutralizes the virulence of and exhibits therapeutic efficacy in a murine candidiasis model. These findings support the application of CBS as a potential therapeutic target to fight fungal infections.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9757746 | PMC |
| http://dx.doi.org/10.1126/sciadv.add5366 | DOI Listing |
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