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Secretory proteins are delivered to the septin-organized penetration interface during root infection by Verticillium dahliae
by
Zhao, Yun-Long
, Zhou, Ting-Ting
, Guo, Hui-Shan
in
Analysis
/ Binding proteins
/ Biology and Life Sciences
/ Cotton
/ Effectors
/ Fluorescence Recovery After Photobleaching
/ Fungal Proteins - metabolism
/ Fungi
/ Gene Knockout Techniques
/ Genomics
/ Gossypium - parasitology
/ Host plants
/ Host-parasite relationships
/ Host-Pathogen Interactions - physiology
/ Hyphae - ultrastructure
/ Immunity
/ Infections
/ Laboratories
/ Life sciences
/ Localization
/ Microscopy, Electron, Transmission
/ Mutants
/ Mutation
/ NAD(P)H oxidase
/ Oxidase
/ Pathogens
/ Penetration
/ Phytopathogenic fungi
/ Plant diseases
/ Plant Diseases - parasitology
/ Plant immunity
/ Plant Roots - parasitology
/ Polyethylene glycol
/ Proteins
/ Real-Time Polymerase Chain Reaction
/ Research and Analysis Methods
/ Roots
/ Septin
/ Septins - metabolism
/ Tagging
/ Verticillium
/ Verticillium - pathogenicity
/ Verticillium - ultrastructure
/ Virulence
2017
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Secretory proteins are delivered to the septin-organized penetration interface during root infection by Verticillium dahliae
by
Zhao, Yun-Long
, Zhou, Ting-Ting
, Guo, Hui-Shan
in
Analysis
/ Binding proteins
/ Biology and Life Sciences
/ Cotton
/ Effectors
/ Fluorescence Recovery After Photobleaching
/ Fungal Proteins - metabolism
/ Fungi
/ Gene Knockout Techniques
/ Genomics
/ Gossypium - parasitology
/ Host plants
/ Host-parasite relationships
/ Host-Pathogen Interactions - physiology
/ Hyphae - ultrastructure
/ Immunity
/ Infections
/ Laboratories
/ Life sciences
/ Localization
/ Microscopy, Electron, Transmission
/ Mutants
/ Mutation
/ NAD(P)H oxidase
/ Oxidase
/ Pathogens
/ Penetration
/ Phytopathogenic fungi
/ Plant diseases
/ Plant Diseases - parasitology
/ Plant immunity
/ Plant Roots - parasitology
/ Polyethylene glycol
/ Proteins
/ Real-Time Polymerase Chain Reaction
/ Research and Analysis Methods
/ Roots
/ Septin
/ Septins - metabolism
/ Tagging
/ Verticillium
/ Verticillium - pathogenicity
/ Verticillium - ultrastructure
/ Virulence
2017
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Secretory proteins are delivered to the septin-organized penetration interface during root infection by Verticillium dahliae
by
Zhao, Yun-Long
, Zhou, Ting-Ting
, Guo, Hui-Shan
in
Analysis
/ Binding proteins
/ Biology and Life Sciences
/ Cotton
/ Effectors
/ Fluorescence Recovery After Photobleaching
/ Fungal Proteins - metabolism
/ Fungi
/ Gene Knockout Techniques
/ Genomics
/ Gossypium - parasitology
/ Host plants
/ Host-parasite relationships
/ Host-Pathogen Interactions - physiology
/ Hyphae - ultrastructure
/ Immunity
/ Infections
/ Laboratories
/ Life sciences
/ Localization
/ Microscopy, Electron, Transmission
/ Mutants
/ Mutation
/ NAD(P)H oxidase
/ Oxidase
/ Pathogens
/ Penetration
/ Phytopathogenic fungi
/ Plant diseases
/ Plant Diseases - parasitology
/ Plant immunity
/ Plant Roots - parasitology
/ Polyethylene glycol
/ Proteins
/ Real-Time Polymerase Chain Reaction
/ Research and Analysis Methods
/ Roots
/ Septin
/ Septins - metabolism
/ Tagging
/ Verticillium
/ Verticillium - pathogenicity
/ Verticillium - ultrastructure
/ Virulence
2017
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Secretory proteins are delivered to the septin-organized penetration interface during root infection by Verticillium dahliae
Journal Article
Secretory proteins are delivered to the septin-organized penetration interface during root infection by Verticillium dahliae
2017
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Overview
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.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Cotton
/ Fluorescence Recovery After Photobleaching
/ Fungal Proteins - metabolism
/ Fungi
/ Genomics
/ Host-Pathogen Interactions - physiology
/ Immunity
/ Microscopy, Electron, Transmission
/ Mutants
/ Mutation
/ Oxidase
/ Plant Diseases - parasitology
/ Proteins
/ Real-Time Polymerase Chain Reaction
/ Research and Analysis Methods
/ Roots
/ Septin
/ Tagging
/ Verticillium - pathogenicity
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