ApWD40a, a Member of the WD40-Repeat Protein Family, Is Crucial for Fungal Development, Toxin Synthesis, and Pathogenicity in the Ginseng Alternaria Leaf Blight Fungus <i>Alternaria panax</i>
<i>Alternaria panax</i>, the primary pathogen that causes ginseng Alternaria leaf blight disease, can lead to a 20–30% reduction in ginseng yield. WD40 repeat-containing proteins are evolutionarily conserved proteins with diverse functions between different organisms. In this study, we c...
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| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-01-01
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| Series: | Journal of Fungi |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2309-608X/11/1/59 |
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| Summary: | <i>Alternaria panax</i>, the primary pathogen that causes ginseng Alternaria leaf blight disease, can lead to a 20–30% reduction in ginseng yield. WD40 repeat-containing proteins are evolutionarily conserved proteins with diverse functions between different organisms. In this study, we characterized the roles of a WD40 repeat-containing protein in <i>A. panax</i>. The deletion of <i>ApWD40a</i> impaired the mycelial growth, reduced the sporulation, and significantly decreased the efficiency in utilizing various carbon sources. The Δ<i>Apwd40a</i> mutant showed increased sensitivity to osmotic stress and metal ion stress induced by sorbitol, NaCl, and KCl, but decreased the sensitivity to a cell wall stress factor (SDS) and oxidative stress factors (paraquat and H<sub>2</sub>O<sub>2</sub>). Pathogenicity assays performed on detached ginseng leaves and roots revealed that the disruption of <i>ApWD40a</i> significantly decreased the fungal virulence through attenuating melanin and mycotoxin production by <i>A. panax</i>. A comparative transcriptome analysis revealed that <i>ApWD40a</i> was involved in many metabolic and biosynthetic processes, including amino acid metabolism, carbon metabolism, sulfate metabolic pathways, and secondary metabolite pathways. In particular, a significantly upregulated gene that encoded a sulfate permease 2 protein in Δ<i>Apwd40a</i>, named <i>ApSulP2</i>, was deleted in the wild-type strain of <i>A. panax</i>. The deletion of <i>ApSulP2</i> resulted in reduced biomass under sulfate-free conditions, demonstrating that the sulfate transport was impaired. Taken together, our findings highlight that <i>ApWD40a</i> played crucial roles in different biological processes and the pathogenicity of <i>A. panax</i> through modulating the expressions of genes involved in various primary and secondary metabolic processes. |
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| ISSN: | 2309-608X |