Comparative S-acyl-proteomics reveals post-translational modulation of fungal purine metabolism for Verticillium wilt
- 1Guangdong Provincial Key Laboratory of Biotechnology for Plant Development, School of Life Sciences, South China Normal University, Guangzhou, China
- 2Guangdong Key Laboratory for Crop Germplasm Resources Preservation and Utilization, Agro-biological Gene Research Center, Guangdong Academy of Agricultural Sciences, Guangzhou, China
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.
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BibTeX
@article{li2026comparative,
title = {{Comparative S-acyl-proteomics reveals post-translational modulation of fungal purine metabolism for Verticillium wilt}},
author = {Chi Li and Wenyang Zhang and Shuaifei Cui and Jian Zhang and Yuzhen Li and Xiaoshi Liu and Yang Li and Zhiying Wang and Wenjie Huang and Gongda Li and Chengwei Yang and Shijuan Yan and Jianbin Lai},
journal = {PLOS Pathogens},
year = {2026},
month = oct,
doi = {10.1371/journal.ppat.1014730},
url = {https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1014730},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Comparative S-acyl-proteomics reveals post-translational modulation of fungal purine metabolism for Verticillium wilt
AU - Chi Li
AU - Wenyang Zhang
AU - Shuaifei Cui
AU - Jian Zhang
AU - Yuzhen Li
AU - Xiaoshi Liu
AU - Yang Li
AU - Zhiying Wang
AU - Wenjie Huang
AU - Gongda Li
AU - Chengwei Yang
AU - Shijuan Yan
AU - Jianbin Lai
PY - 2026
DA - 2026/10/26
JO - PLOS Pathogens
DO - 10.1371/journal.ppat.1014730
UR - https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1014730
AB - 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.
SN - 1553-7374
SN - 1553-7366
ER -