ArticleCommunications biology2022
Integrated omics approach to unveil antifungal bacterial polyynes as acetyl-CoA acetyltransferase inhibitors.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Defining the cultured and uncultured bacterial fractions in Cannabis seeds.Environmental microbiome · 2025Article
- Polyyne production is regulated by the transcriptional regulators PgnC and GacA inApplied and environmental microbiology · 2025Article
- Targeting fungal lipid synthesis for antifungal drug development and potentiation of contemporary antifungals.npj antimicrobials and resistance · 2025Review
- Elucidation of Antimicrobials and Biofilm Inhibitors Derived from a Polyacetylene Core.Molecules (Basel, Switzerland) · 2024Article
- Nano-Hybrid Ag@LCCs Systems with Potential Wound-Healing Properties.Materials (Basel, Switzerland) · 2023Article
- Polyyne-producingFrontiers in microbiology · 2023Article
- Mechanistic insights of magnolol antimicrobial activity againstFrontiers in cellular and infection microbiology · 2023Article
- Discovery, mode of action and secretion ofCell surface (Amsterdam, Netherlands) · 2022Review
- Thiotemplated Biosynthesis of Bacterial Polyyne Fatty Acids by a Designated Desaturase Triad.Chembiochem : a European journal of chemical biology · 2022Article
Corrections and comments
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Authors and funding
14 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial polyynes are highly active natural products with a broad spectrum of antimicrobial activities. However, their detailed mechanism of action remains unclear. By integrating comparative genomics, transcriptomics, functional genetics, and metabolomics analysis, we identified a unique polyyne resistance gene, masL (encoding acetyl-CoA acetyltransferase), in the biosynthesis gene cluster of antifungal polyynes (massilin A 1, massilin B 2, collimonin C 3, and collimonin D 4) of Massilia sp. YMA4. Crystallographic analysis indicated that bacterial polyynes serve as covalent inhibitors of acetyl-CoA acetyltransferase. Moreover, we confirmed that the bacterial polyynes disrupted cell membrane integrity and inhibited the cell viability of Candida albicans by targeting ERG10, the homolog of MasL. Thus, this study demonstrated that acetyl-CoA acetyltransferase is a potential target for developing antifungal agents.
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