{ "abstract": "Verticillium wilt, caused by the fungus Verticillium dahliae, is a devastating plant disease leading to severe global agricultural losses. Although the interaction between V. dahliae and host plants has been extensively investigated, the role of metabolic regulation in fungal development and pathogenicity remains poorly understood. Fatty acids serve as metabolic substrates for S-acylation, a post-translational modification that modulates protein properties and functions, yet this process has not been characterized in V. dahliae. Here, our systematic analysis revealed that the protein S-acyltransferase VdERF2 is essential for the development and pathogenicity of V. dahliae. Through comparative S-acyl-proteomic analyses, we found that VdERF2-dependent S-acylation is significantly enriched in metabolic pathways, especially purine metabolism. Among the identified substrates, VdHIUH, an enzyme involved in converting uric acid to allantoin in purine metabolism, requires S-acylation for its full function in fungal development and virulence. VdERF2-mediated S-acylation enhances the activity of VdHIUH, thereby reducing uric acid accumulation. Furthermore, allantoin reduces reactive oxygen species elevated by the VdHIUH S-acylation defect, partially alleviating the fungal developmental impairment. Collectively, our findings reveal a critical mechanism by which S-acylation modulates purine metabolism in V. dahliae, providing new insights into the molecular basis of fungal pathogenicity and offering potential targets for improving crop resistance to Verticillium wilt. Author summary: Verticillium wilt, which is caused by Verticillium dahliae, is a important global plant disease. However, the role of metabolic regulation in the growth and pathogenicity of this plant pathogenic fungus remains unclear. S-acylation, is a key post-translational modification which transfers fatty acids to protein substrates, but it has not been characterized in V. dahliae. Here, we show that the protein S-acyltransferase VdERF2 is essential for V. dahliae development and virulence. Comparative S-acyl-proteomics reveals VdERF2-dependent S-acylation is enriched in metabolism-associated processes, especially purine metabolism. Among its substrates, VdHIUH, the enzyme converting uric acid to allantoin, requires S-acylation for full activity, supporting normal development and pathogenicity. VdERF2-mediated S-acylation enhances VdHIUH activity, lowering uric acid accumulation. Notably, exogenous allantoin partially alleviates developmental defects caused by impaired VdHIUH S-acylation in V. dahliae, likely by suppressing the accumulation of reactive oxygen species. Together, these findings uncover an S-acylation-purine metabolism axis governing V. dahliae virulence, and identify promising new targets for Verticillium wilt control.", "abstract_shown": true, "affiliations": [ "Guangdong Provincial Key Laboratory of Biotechnology for Plant Development, School of Life Sciences, South China Normal University, Guangzhou, China", "Guangdong Key Laboratory for Crop Germplasm Resources Preservation and Utilization, Agro-biological Gene Research Center, Guangdong Academy of Agricultural Sciences, Guangzhou, China" ], "article_type": "Research Article", "arxiv": null, "author_total": 13, "authors": [ { "affs": [ 0 ], "name": "Chi Li" }, { "affs": [ 1 ], "name": "Wenyang Zhang" }, { "affs": [ 0 ], "name": "Shuaifei Cui" }, { "affs": [ 0 ], "name": "Jian Zhang" }, { "affs": [ 0 ], "name": "Yuzhen Li" }, { "affs": [ 0 ], "name": "Xiaoshi Liu" }, { "affs": [ 0 ], "name": "Yang Li" }, { "affs": [ 0 ], "name": "Zhiying Wang" }, { "affs": [ 1 ], "name": "Wenjie Huang" }, { "affs": [ 0 ], "name": "Gongda Li" }, { "affs": [ 0 ], "name": "Chengwei Yang" }, { "affs": [ 1 ], "name": "Shijuan Yan" }, { "affs": [ 0 ], "name": "Jianbin Lai", "orcid": "0000-0002-9269-9052" } ], "bibtex": "https://research.draconitic.com/paper/0h8c4t08zfe12.bib", "cited_by": 0, "doi": "10.1371/journal.ppat.1014730", "fulltext_url": "https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1014730", "id": "0h8c4t08zfe12", "issns": [ "1553-7374", "1553-7366" ], "landing_url": "https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1014730", "language": "en", "licence": "CC-BY-4.0", "licence_label": "CC BY 4.0", "licence_source": "article", "licence_url": "https://creativecommons.org/licenses/by/4.0/", "metadata_licence": null, "native_subjects": [ [ "heading", "Acids" ], [ "heading", "Biochemistry" ], [ "heading", "Biology and Life Sciences" ], [ "heading", "Chemical Compounds" ], [ "heading", "Chemistry" ], [ "heading", "Cotton" ], [ "heading", "Enzyme Chemistry" ], [ "heading", "Enzyme Regulation" ], [ "heading", "Enzymology" ], [ "heading", "Eukaryota" ], [ "heading", "Flowering Plants" ], [ "heading", "Medicine and Health Sciences" ], [ "heading", "Metabolism" ], [ "heading", "Organisms" ], [ "heading", "Pathogenesis" ], [ "heading", "Pathology and Laboratory Medicine" ], [ "heading", "Physical Sciences" ], [ "heading", "Plant Fungal Pathogens" ], [ "heading", "Plant Pathogens" ], [ "heading", "Plant Pathology" ], [ "heading", "Plant Science" ], [ "heading", "Plants" ], [ "heading", "Protein Metabolism" ], [ "heading", "Purine Metabolism" ], [ "heading", "Research Article" ], [ "heading", "Uric Acid" ], [ "openalex", "1312|Fungal and yeast genetics research" ], [ "plos", "/Biology and life sciences/Biochemistry/Enzymology/Enzyme chemistry/Enzyme regulation" ], [ "plos", "/Biology and life sciences/Biochemistry/Metabolism/Protein metabolism" ], [ "plos", "/Biology and life sciences/Biochemistry/Metabolism/Purine metabolism" ], [ "plos", "/Biology and life sciences/Organisms/Eukaryota/Plants/Flowering plants/Cotton" ], [ "plos", "/Biology and life sciences/Plant science/Plant pathology" ], [ "plos", "/Biology and life sciences/Plant science/Plant pathology/Plant pathogens/Plant fungal pathogens" ], [ "plos", "/Medicine and health sciences/Pathology and laboratory medicine/Pathogenesis" ], [ "plos", "/Physical sciences/Chemistry/Chemical compounds/Acids/Uric acid" ] ], "openalex": "W7223679240", "pdf_url": "https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1014730&type=printable", "pmcid": "PMC13722310", "pmid": "42932396", "published": "2026-10-26", "publisher": "Public Library of Science", "ris": "https://research.draconitic.com/paper/0h8c4t08zfe12.ris", "sources": [ { "first_seen": "2026-10-30T12:17:17Z", "native_id": "10.1371/journal.ppat.1014730", "source": "plos", "url": "https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1014730" }, { "first_seen": "2026-11-03T12:22:50Z", "native_id": "PMC13722310", "source": "pmc", "url": "https://doi.org/10.1371/journal.ppat.1014730" } ], "subjects": [ { "field": "biochemistry", "origin": "plos:enzymology", "subfield": "enzymology-metabolism" }, { "field": "biology", "origin": "plos:plant science", "subfield": "plant-biology" }, { "field": "chemistry", "origin": "heading:Chemistry", "subfield": "general" }, { "field": "medicine", "origin": "heading:Medicine and Health Sciences", "subfield": "general" } ], "title": "Comparative S-acyl-proteomics reveals post-translational modulation of fungal purine metabolism for Verticillium wilt", "title_text": "Comparative S-acyl-proteomics reveals post-translational modulation of fungal purine metabolism for Verticillium wilt", "type": "peer-reviewed", "updated_at": "2026-11-03T12:22:50Z", "url": "https://research.draconitic.com/paper/0h8c4t08zfe12", "venue": "PLOS Pathogens", "versions": [] }