ArticleNature communications2025
Mechanisms of aureobasidin A inhibition and drug resistance in a fungal IPC synthase complex.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Cyclic Peptides in Modern Drug Discovery: Trends and Therapeutic Directions.Journal of medicinal chemistry · 2026Review
- FpLaeA Coordinates Fusarium proliferatum Pathogenesis by Orchestrating Mycotoxin Biosynthesis and Host Immune Subversion.Journal of agricultural and food chemistry · 2026Article
- Molecular insights into fungal inositol phosphorylceramide synthesis and its inhibition by antifungal aureobasidin A.Nature communications · 2026Article
- Overcoming antifungal resistance inFrontiers in cellular and infection microbiology · 2025Review
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Authors and funding
3 authors.
Funding
Abstract
The enzyme inositol phosphorylceramide (IPC) synthase is essential for survival and virulence in fungi, while absent in mammals, thus representing a potential target for antifungal treatments. Aureobasidin A (AbA), a natural cyclic peptide, displays antifungal activity and inhibits IPC synthase, but the precise molecular mechanism remains unclear. Here, we present the cryo-EM structure of the Saccharomyces cerevisiae IPC synthase, composed of catalytic subunit Aur1 and regulatory subunit Kei1, in its AbA-bound state. The complex is resolved as a dimer of Aur1-Kei1 heterodimers, with Aur1 mediating homodimerization. AbA occupies a predominantly hydrophobic pocket in the catalytic core domain of each Aur1 subunit, blocking the entry of both substrates. Mutations conferring AbA resistance cluster near the AbA-binding site, thus interfering with AbA binding. Our study lays a foundation for the development of therapeutic drugs targeting fungal IPC synthase.
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