ArticlePLoS pathogens2017
Secretory proteins are delivered to the septin-organized penetration interface during root infection by Verticillium dahliae.
Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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52 citing papers in PubMed, 101 citations in OpenAlex.
- Multiple environmental test and genetic mapping jointly reveal genomic loci and associated genes underlying cotton Verticillium wilt resistance.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026Article
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- GhPsbO breaks the growth-immunity tradeoff by simultaneously promoting growth and defense in cotton.The Plant cell · 2026Article
- The Aromatic Amino Acid Biosynthesis GeneMicroorganisms · 2025Article
- A fungal pathogen manipulates phytocytokine signaling for plant infection.Nature communications · 2025Article
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- CWI-MAPKs Regulate the Formation of Hyphopodia Required for Virulence in Ceratocystis fimbriata.Molecular plant pathology · 2025Article
- Verticillium dahliae Secretory Aspartyl Protease VdSAP Targets Cotton GhARP to Modulate Plant Defence and Defoliation.Molecular plant pathology · 2025Article
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- The Exocyst Subunits EqSec5 and EqSec6 Promote Powdery Mildew Fungus Growth and Pathogenicity.Journal of fungi (Basel, Switzerland) · 2025Article
- Recognition of a Fungal Effector Potentiates Pathogen-Associated Molecular Pattern-Triggered Immunity in Cotton.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Natural SNP Variation in GbOSM1 Promotor Enhances Verticillium Wilt Resistance in Cotton.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- The Kelch Repeat Protein VdKeR1 Is Essential for Development, Ergosterol Metabolism, and Virulence inJournal of fungi (Basel, Switzerland) · 2024Article
- Fimbrin associated with Pmk1 to regulate the actin assembly during Magnaporthe oryzae hyphal growth and infection.Stress biology · 2024Article
- DeSUMOylation of a Verticillium dahliae enolase facilitates virulence by derepressing the expression of the effector VdSCP8.Nature communications · 2023Article
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- Hyphopodium-Specific Signaling Is Required for Plant Infection byJournal of fungi (Basel, Switzerland) · 2023Article
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- Hypothetical Protein VDAG_07742 Is Required forInternational journal of molecular sciences · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Successful infection of the host requires secretion of effector proteins to evade or suppress plant immunity. Secretion of effectors in root-infecting fungal pathogens, however, remains unexplored. We previously reported that Verticillium dahliae, a root-infecting phytopathogenic fungus, develops a penetration peg from a hyphopodium to infect cotton roots. In this study, we report that a septin ring, requiring VdSep5, partitions the hyphopodium and the invasive hypha and form the specialized fungus-host interface. The mutant strain, VdΔnoxb, in which NADPH oxidase B (VdNoxB) is deleted, impaired formation of the septin ring at the hyphal neck, indicating that NADPH oxidases regulate septin ring organization. Using GFP tagging and live cell imaging, we observed that several signal peptide containing secreted proteins showed ring signal accumulation/secretion at the penetration interface surrounding the hyphal neck. Targeted mutation for VdSep5 reduced the delivery rate of secretory proteins to the penetration interface. Blocking the secretory pathway by disrupting the vesicular trafficking factors, VdSec22 and VdSyn8, or the exocyst subunit, VdExo70, also arrested delivery of the secreted proteins inside the hyphopodium. Reduced virulence was observed when cotton roots were infected with VdΔsep5, VdΔsec22, VdΔsyn8 and VdΔexo70 mutants compared to infection with the isogenic wild-type V592. Taken together, our data demonstrate that the hyphal neck is an important site for protein secretion during plant root infection, and that the multiple secretory routes are involved in the secretion.
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