An Antifungal with a Novel Mechanism of Action Discovered via Resistance Gene-Guided Genome Mining

Read full text
Authors: Bruno Perlatti, Sandeep Vellanki, Yalong Zhang, Yi‐Ming Chiang, Yingxia Hu, Mengdi Yuan, Kyle L. Dunbar, Abigail Fine, Michelle F. Grau, Sheena C. Li, Timothy J. O’Donnell, Rajani M. Shenoy
+9 more Hongtao Li, Hui Shi, Xia Xu, Zeyu Chen, Tara Arvedson, Yi Fan Tang, R. Cramer, Victor J. Cee, Colin J. B. Harvey
Cited by: 3
References: 46

Abstract

High Resolution Image Download MS PowerPoint Slide Invasive fungal infections claim over two million lives annually, a problem exacerbated by rising resistance to current antifungal treatments and an increasing population of immunocompromised individuals. Despite this, antifungal drug development has stagnated, with few novel agents and fewer novel targets explored in recent decades. Here, we validate acetolactate synthase (ALS), an enzyme critical for branched-chain amino acid biosynthesis and absent in humans, as a promising target for new therapeutics. Using resistance gene-guided genome mining, we discovered a biosynthetic gene cluster in Aspergillus terreus encoding HB-35018 (1), a novel spiro-cis-decalin tetramic acid that potently inhibits ALS. Biochemical and antifungal assays demonstrate that 1 surpasses existing ALS inhibitors in efficacy against Aspergillus fumigatus and other pathogenic fungi. Structural studies via cryo-electron microscopy reveal a unique covalent binding interaction between compound 1 and ALS, distinct from known inhibitors, and finally, we demonstrate that ALS is essential for virulence in a mouse model of invasive aspergillosis. These findings position ALS as a promising target for antifungal development and demonstrate the potential of resistance gene-guided genome mining for antifungal discovery.

Fields of Study & Subjects

Microbial Natural Products and Biosynthesis Antifungal resistance and susceptibility Peptidase Inhibition and Analysis

Publication details

Journal / source
ACS Central Science
Publisher
American Chemical Society (ACS)
Volume
12
Issue
2
Pages
197–207
Publication date
31 January 2026
Language
EN