scholarly journals Chitosan inhibits septin‐mediated plant infection by the rice blast fungus Magnaporthe oryzae in a protein kinase C and Nox1 NADPH oxidase‐dependent manner

2021 ◽  
Vol 230 (4) ◽  
pp. 1578-1593
Author(s):  
Federico Lopez‐Moya ◽  
Magdalena Martin‐Urdiroz ◽  
Miriam Oses‐Ruiz ◽  
Vincent M. Were ◽  
Mark D. Fricker ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nadph Oxidase ◽  
Magnaporthe Oryzae ◽  
Rice Blast ◽  
Rice Blast Fungus ◽  
Dependent Manner ◽  
Plant Infection ◽  
Kinase C ◽  
Blast Fungus

scholarly journals Chitosan inhibits septin-mediated plant infection by the rice blast fungus Magnaporthe oryzae in a Protein Kinase C and Nox1 NADPH oxidase-dependent manner

2020 ◽  
Author(s):  
Federico Lopez-Moya ◽  
Magdalena Martin-Urdiroz ◽  
Miriam Oses-Ruiz ◽  
Mark D. Fricker ◽  
George R. Littlejohn ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Protein Kinase C ◽  
Nadph Oxidase ◽  
Rice Blast ◽  
Rice Blast Fungus ◽  
Plant Infection ◽  
Kinase C ◽  
Blast Fungus ◽  
Cell Wall Integrity Pathway

SummaryChitosan is a partially deacetylated linear polysaccharide composed of β-1,4-linked units of D-glucosamine and N-acetyl glucosamine. As well as acting as a structural component of fungal cell walls, chitosan can be applied as a potent antifungal agent. However, the mode-of-action of chitosan in fungal pathogens is poorly understood.Here, we report that chitosan is effective for control of rice blast disease. Chitosan application impairs growth of the blast fungus Magnaporthe oryzae and has a pronounced effect on appressorium-mediated plant infection. Chitosan inhibits septin-mediated F-actin re-modelling at the appressorium pore, thereby preventing re-polarisation of the infection cell and rice leaf cuticle penetration.We found that chitosan causes plasma membrane permeabilization of M. oryzae and affects NADPH oxidase-dependent synthesis of reactive oxygen species, essential for septin ring formation and fungal pathogenicity. Our data further show that the toxicity of chitosan to M. oryzae requires the protein kinase C-dependent cell wall integrity pathway and the Nox1 NADPH oxidase. A conditionally lethal, analogue (PP1)-sensitive mutant of Pkc1 is partially remediated for growth in the presence of chitosan and PP1, while Δnox1 mutants increase their glucan/chitin cell wall ratio, rendering them resistant to chitosan.Taken together, our data show that chitosan is a potent fungicide for control of the rice blast fungus which involves the cell wall integrity pathway, disrupts plasma membrane and inhibits septin-mediated plant infection.

scholarly journals Protein kinase C is essential for viability of the rice blast fungus M agnaporthe oryzae

2015 ◽  
Vol 98 (3) ◽  
pp. 403-419 ◽  
Author(s):  
Tina J. Penn ◽  
Mark E. Wood ◽  
Darren M. Soanes ◽  
Michael Csukai ◽  
Andrew John Corran ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rice Blast ◽  
Rice Blast Fungus ◽  
Kinase C ◽  
Blast Fungus

scholarly journals Investigating the cell and developmental biology of plant infection by the rice blast fungus Magnaporthe oryzae

2021 ◽  
pp. 103562
Author(s):  
Alice Bisola Eseola ◽  
Lauren S. Ryder ◽  
Míriam Osés-Ruiz ◽  
Kim Findlay ◽  
Xia Yan ◽  
...  
Keyword(s):  
Developmental Biology ◽  
Magnaporthe Oryzae ◽  
Rice Blast ◽  
Rice Blast Fungus ◽  
Plant Infection ◽  
Blast Fungus

scholarly journals MoSnt2-dependent deacetylation of histone H3 mediates MoTor-dependent autophagy and plant infection by the rice blast fungus Magnaporthe oryzae

Autophagy ◽  
2018 ◽  
Vol 14 (9) ◽  
pp. 1543-1561 ◽  
Author(s):  
Min He ◽  
Youpin Xu ◽  
Jinhua Chen ◽  
Yuan Luo ◽  
Yang Lv ◽  
...  
Keyword(s):  
Magnaporthe Oryzae ◽  
Rice Blast ◽  
Histone H3 ◽  
Rice Blast Fungus ◽  
Plant Infection ◽  
Blast Fungus

scholarly journals Structure-Function Analysis of a CVNH-LysM Lectin Expressed during Plant Infection by the Rice Blast Fungus Magnaporthe oryzae

Structure ◽  
2011 ◽  
Vol 19 (5) ◽  
pp. 662-674 ◽  
Author(s):  
Leonardus M.I. Koharudin ◽  
Arturo R. Viscomi ◽  
Barbara Montanini ◽  
Michael J. Kershaw ◽  
Nicholas J. Talbot ◽  
...  
Keyword(s):  
Structure Function ◽  
Magnaporthe Oryzae ◽  
Rice Blast ◽  
Function Analysis ◽  
Rice Blast Fungus ◽  
Plant Infection ◽  
Blast Fungus

Investigating the biology of plant infection by the rice blast fungus Magnaporthe oryzae

2016 ◽  
Vol 90 ◽  
pp. 61-68 ◽  
Author(s):  
Magdalena Martin-Urdiroz ◽  
Miriam Oses-Ruiz ◽  
Lauren S. Ryder ◽  
Nicholas J. Talbot
Keyword(s):  
Magnaporthe Oryzae ◽  
Rice Blast ◽  
Rice Blast Fungus ◽  
Plant Infection ◽  
Blast Fungus

scholarly journals MoRic8 Is a Novel Component of G-Protein Signaling During Plant Infection by the Rice Blast Fungus Magnaporthe oryzae

2010 ◽  
Vol 23 (3) ◽  
pp. 317-331 ◽  
Author(s):  
Ya Li ◽  
Xia Yan ◽  
Hong Wang ◽  
Shen Liang ◽  
Wei-Bin Ma ◽  
...  
Keyword(s):  
G Protein ◽  
Magnaporthe Oryzae ◽  
Rice Blast ◽  
Insertional Mutagenesis ◽  
Rice Blast Fungus ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Targeted Gene Deletion ◽  
Plant Infection ◽  
Blast Fungus

An insertional mutagenesis screen was used to investigate the biology of plant infection by the devastating rice blast pathogen, Magnaporthe oryzae. Here, we report the identification of a new mutant, LY-130, which is defective in multiple steps during infection-related morphogenesis and pathogenicity. Analysis of the mutation confirmed an insertion into gene MoRIC8, which encodes a 480-amino-acid protein that is a putative homologue of the Ric8 regulator of GTP-binding protein (G-protein) signaling, previously described in animals. Targeted gene deletion mutants of MoRIC8 were nonpathogenic and impaired in cellular differentiation associated with sporulation, sexual development, and plant infection. MoRic8 physically interacts with the Gα subunit MagB in yeast two-hybrid assays and appears to act upstream of the cyclic AMP response pathway that is necessary for appressorium morphogenesis. Taken together, our results indicate that MoRic8 may act as a novel regulator of the G-protein signaling during infection-related development of rice blast fungus M. oryzae.

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