ArticleScientific reports2019
Substitution of cysteines in the yeast viral killer toxin K1 precursor reveals novel insights in heterodimer formation and immunity.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Antimicrobial Effect of Silver Nanoparticles Capped withNanomaterials (Basel, Switzerland) · 2026Article
- Alanine scanning of the yeast killer toxin K2 reveals key residues for activity, gain-of-function variants, and supports prediction of precursor processing and 3D structure.Journal of structural biology: X · 2026Article
- Extrachromosomally co-encoded toxin-immunity pairs in yeast and their application potential.Applied microbiology and biotechnology · 2026Review
- Article
- ThemBio · 2025Article
- A Comprehensive Structural and Functional Analysis ofbioRxiv : the preprint server for biology · 2025Article
- Overcoming toxicity: How nonantagonistic microbes manage to thrive in boom-and-bust environments.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The KillerMicroorganisms · 2024Review
- The Viral K1 Killer Yeast System: Toxicity, Immunity, and Resistance.Yeast (Chichester, England) · 2024Review
- The evolutionary ecology of fungal killer phenotypes.Proceedings. Biological sciences · 2023Review
- Expression of the K74 Killer Toxin from Saccharomyces paradoxus Is Modulated by the Toxin-Encoding M74 Double-Stranded RNA 5' Untranslated Terminal Region.Applied and environmental microbiology · 2022Article
- The Species-Specific Acquisition and Diversification of a K1-like Family of Killer Toxins in Budding Yeasts of the Saccharomycotina.PLoS genetics · 2021Article
- Analysis of Yeast Killer Toxin K1 Precursor Processing via Site-Directed Mutagenesis: Implications for Toxicity and Immunity.mSphere · 2020Article
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4 authors.
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Abstract
The killer toxin K1 is a virally encoded fungal A/B toxin acting by disrupting plasma membrane integrity. The connection of α and β constitutes a critical feature for toxin biology and for decades the formation of three disulphide bonds linking the major toxin subunits was accepted as status quo. Due to the absence of experimental evidence, the involvement of each cysteine in heterodimer formation, K1 lethality and immunity was systematically analysed. Substitution of any cysteine in α led to a complete loss of toxin dimer secretion and toxicity, whereas K1 toxin derivatives carrying mutations of C248, C312 or the double mutation C248-312 were active against spheroplasted cells. Importantly, substitution of the C95 and C107 in the toxin precursor completely abolished the mediation of functional immunity. In contrast, K1 toxicity, i.e. its ionophoric effect, does not depend on the cysteine residues at all. In contrast to the literature, our data imply the formation of a single disulphide bond involving C92 in α and C239 in β. This finding not only refines the current model stated for decades but also provides new opportunities to elucidate the mechanisms underlying K1 toxicity and immunity at the molecular level.
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