GPI7-mediated glycosylphosphatidylinositol anchoring regulates appressorial penetration and immune evasion during infection of Magnaporthe oryzae.
Ascomycota
/ genetics
Cell Wall
/ metabolism
Chitin
/ metabolism
Fungal Proteins
/ genetics
Glucans
/ metabolism
Glycosylphosphatidylinositols
/ metabolism
Hydrofluoric Acid
/ pharmacology
Hyphae
/ metabolism
Oryza
/ microbiology
Phosphotransferases
/ genetics
Plant Diseases
/ microbiology
Virulence
Journal
Environmental microbiology
ISSN: 1462-2920
Titre abrégé: Environ Microbiol
Pays: England
ID NLM: 100883692
Informations de publication
Date de publication:
07 2020
07 2020
Historique:
received:
02
07
2019
accepted:
12
02
2020
pubmed:
18
2
2020
medline:
26
1
2021
entrez:
18
2
2020
Statut:
ppublish
Résumé
Glycosylphosphatidylinositol (GPI) anchoring plays key roles in many biological processes by targeting proteins to the cell wall; however, its roles are largely unknown in plant pathogenic fungi. Here, we reveal the roles of the GPI anchoring in Magnaporthe oryzae during plant infection. The GPI-anchored proteins were found to highly accumulate in appressoria and invasive hyphae. Disruption of GPI7, a GPI anchor-pathway gene, led to a significant reduction in virulence. The Δgpi7 mutant showed significant defects in penetration and invasive growth. This mutant also displayed defects of the cell wall architecture, suggesting GPI7 is required for cell wall biogenesis. Removal of GPI-anchored proteins in the wild-type strain by hydrofluoric acid (HF) pyridine treatment exposed both the chitin and β-1,3-glucans to the host immune system. Exposure of the chitin and β-1,3-glucans was also observed in the Δgpi7 mutant, indicating GPI-anchored proteins are required for immune evasion. The GPI anchoring can regulate subcellular localization of the Gel proteins in the cell wall for appressorial penetration and abundance of which for invasive growth. Our results indicate the GPI anchoring facilitates the penetration of M. oryzae into host cells by affecting the cell wall integrity and the evasion of host immune recognition.
Identifiants
pubmed: 32064718
doi: 10.1111/1462-2920.14941
doi:
Substances chimiques
Fungal Proteins
0
Glucans
0
Glycosylphosphatidylinositols
0
Chitin
1398-61-4
Phosphotransferases
EC 2.7.-
Hydrofluoric Acid
RGL5YE86CZ
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2581-2595Subventions
Organisme : Open Research Fund of State Key Laboratory of Hybrid Rice
ID : 2019KF04
Pays : International
Organisme : National Natural Science Foundation of China
ID : 31601585
Pays : International
Organisme : National Natural Science Foundation of China
ID : 31871909
Pays : International
Informations de copyright
© 2020 Society for Applied Microbiology and John Wiley & Sons Ltd.
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