ArticleProceedings of the National Academy of Sciences of the United States of America2000
A gene encoding a sphingolipid biosynthesis enzyme determines the sensitivity of Saccharomyces cerevisiae to an antifungal plant defensin from dahlia (Dahlia merckii).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 182 citations in OpenAlex.
- WHO Critical Priority Fungi: A Comprehensive Review of Antifungal Resistance, Emerging Therapeutic Strategies, and the Potential of Antifungal Peptides.International journal of molecular sciences · 2026Review
- Genomic and functional insights into the diversity of3 Biotech · 2025Article
- Biological Importance of Complex Sphingolipids and Their Structural Diversity in Budding YeastInternational journal of molecular sciences · 2024Review
- Antifungal Plant Defensins as an Alternative Tool to Combat Candidiasis.Plants (Basel, Switzerland) · 2024Review
- Fighting pathogenic yeasts with plant defensins and anti-fungal proteins from fungi.Applied microbiology and biotechnology · 2024Review
- Hyperpolarisation of Mitochondrial Membranes Is a Critical Component of the Antifungal Mechanism of the Plant Defensin, Ppdef1.Journal of fungi (Basel, Switzerland) · 2024Article
- Dual functionality of pathogenesis-related proteins: defensive role in plants versus immunosuppressive role in pathogens.Frontiers in plant science · 2024Article
- Cellular Responses and Targets in Food Spoilage Yeasts Exposed to Antifungal Prenylated Isoflavonoids.Microbiology spectrum · 2023Article
- Pleiotropy drives evolutionary repair of the responsiveness of polarized cell growth to environmental cues.Frontiers in microbiology · 2023Article
- Short Peptides Make a Big Difference: The Role of Botany-Derived AMPs in Disease Control and Protection of Human Health.International journal of molecular sciences · 2021Review
- Membrane-Interacting Antifungal Peptides.Frontiers in cell and developmental biology · 2021Review
- Yeast Sphingolipid-Enriched Domains and Membrane Compartments in the Absence of Mannosyldiinositolphosphorylceramide.Biomolecules · 2020Article
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- Ecotopic Expression of the Antimicrobial Peptide DmAMP1W Improves Resistance of Transgenic Wheat to Two Diseases: Sharp Eyespot and Common Root Rot.International journal of molecular sciences · 2020Article
- Article
- The interaction with fungal cell wall polysaccharides determines the salt tolerance of antifungal plant defensins.Cell surface (Amsterdam, Netherlands) · 2019Article
- Screening theAntimicrobial agents and chemotherapy · 2019Article
- Plant defensins: types, mechanism of action and prospects of genetic engineering for enhanced disease resistance in plants.3 Biotech · 2019Review
- Medicinal Potentialities of Plant Defensins: A Review with Applied Perspectives.Medicines (Basel, Switzerland) · 2019Review
- X-ray structure of a carpet-like antimicrobial defensin-phospholipid membrane disruption complex.Nature communications · 2018Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
We have previously identified a Saccharomyces cerevisiae mutant that is markedly more resistant than wild-type to Dahlia merckii antimicrobial peptide 1 (DmAMP1), an antifungal plant defensin isolated from seeds of dahlia (Dahlia merckii). A complementation approach was followed that consisted of the introduction of a genomic library of DmAMP1-sensitive wild-type yeast into the DmAMP1-resistant yeast mutant and screening for restored sensitivity to DmAMP1. The gene determining sensitivity of S. cerevisiae to DmAMP1 was identified as IPT1, a gene encoding an enzyme involved in the last step of the synthesis of the sphingolipid mannose-(inositol-phosphate)(2)-ceramide. Strains with a nonfunctional IPT1 allele lacked mannose-(inositol-phosphate)(2)-ceramide in their plasma membranes, bound significantly less DmAMP1 compared with wild-type strains, and were highly resistant to DmAMP1-mediated membrane permeabilization. All of these phenotypic deviations could be restored by reintroduction of a functional IPT1 gene. Our data support a model in which membrane patches containing sphingolipids act as binding sites for DmAMP1 or, alternatively, are required to anchor membrane or cell wall-associated proteins, which themselves interact with DmAMP1.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.