Vacuolar Protein-Sorting Receptor MoVps13 Regulates Conidiation and Pathogenicity in Rice Blast Fungus <i>Magnaporthe oryzae</i>

<i>Magnaporthe oryzae</i> (synonym <i>Pyricularia oryzae</i>) is a filamentous fungal pathogen that causes major yield losses in cultivated rice worldwide. However, the mechanisms of infection of <i>M. oryzae</i> are not well characterized. The VPS13 proteins play...

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Main Authors: Xueming Zhu, Lin Li, Jiaoyu Wang, Lili Zhao, Huanbin Shi, Jiandong Bao, Zhenzhu Su, Xiaohong Liu, Fucheng Lin
Format: Article
Language:English
Published: MDPI AG 2021-12-01
Series:Journal of Fungi
Subjects:
Online Access:https://www.mdpi.com/2309-608X/7/12/1084
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author Xueming Zhu
Lin Li
Jiaoyu Wang
Lili Zhao
Huanbin Shi
Jiandong Bao
Zhenzhu Su
Xiaohong Liu
Fucheng Lin
author_facet Xueming Zhu
Lin Li
Jiaoyu Wang
Lili Zhao
Huanbin Shi
Jiandong Bao
Zhenzhu Su
Xiaohong Liu
Fucheng Lin
author_sort Xueming Zhu
collection DOAJ
description <i>Magnaporthe oryzae</i> (synonym <i>Pyricularia oryzae</i>) is a filamentous fungal pathogen that causes major yield losses in cultivated rice worldwide. However, the mechanisms of infection of <i>M. oryzae</i> are not well characterized. The VPS13 proteins play vital roles in various biological processes in many eukaryotic organisms, including in the organization of actin cytoskeleton, vesicle trafficking, mitochondrial fusion, and phagocytosis. Nevertheless, the function of the Vps13 protein in plant pathogenic fungi has not been explored. Here, we analysed the biological functions of the Vps13 protein in the development and pathogenicity of <i>M.</i> <i>oryzae</i>. Deletion mutants of MoVps13 significantly reduced the conidiation and decreased the rate of fungal infection on hosts. Moreover, the loss of MoVps13 resulted in defective cell wall integrity (CWI) and plasma membrane (PM) homeostasis when treated with chemicals for inducing cell wall stress (200 mg/mL Congo Red or 0.005% SDS) and sphingolipid synthesis inhibitors (2 μM myriocin or 2 μM amphotericin B). This indicated that MoVps13 is also involved in cell wall synthesis and sphingolipid synthesis. Through immunoblotting, autophagic flux detection, co-localization, and chemical drug sensitivity assays, we confirmed the involvement of Movps13 in ER-phagy and the response to ER stress. Additionally, we generated the C-terminal structure of MoVps13 with high accuracy using the alphaflod2 database. Our experimental evidence indicates that MoVps13 is an important virulence factor that regulates the pathogenicity of <i>M.</i> <i>oryzae</i> by controlling CWI, lipid metabolism and the ER-phagy pathway. These results have expanded our knowledge about pathogenic fungi and will help exploration for novel therapeutic strategies against the rice blast fungus.
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spelling doaj.art-cf84358f72b048b98c0f1c1d38cabd0e2023-11-23T09:05:36ZengMDPI AGJournal of Fungi2309-608X2021-12-01712108410.3390/jof7121084Vacuolar Protein-Sorting Receptor MoVps13 Regulates Conidiation and Pathogenicity in Rice Blast Fungus <i>Magnaporthe oryzae</i>Xueming Zhu0Lin Li1Jiaoyu Wang2Lili Zhao3Huanbin Shi4Jiandong Bao5Zhenzhu Su6Xiaohong Liu7Fucheng Lin8State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-Products, Institute of Plant Protection and Microbiology, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-Products, Institute of Plant Protection and Microbiology, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-Products, Institute of Plant Protection and Microbiology, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-Products, Institute of Plant Protection and Microbiology, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, ChinaState Key Laboratory of Rice Biology, China National Rice Research Institute, Hangzhou 311499, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-Products, Institute of Plant Protection and Microbiology, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, ChinaState Key Laboratory of Rice Biology, Institute of Biotechnology, Zhejiang University, Hangzhou 310058, ChinaState Key Laboratory of Rice Biology, Institute of Biotechnology, Zhejiang University, Hangzhou 310058, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-Products, Institute of Plant Protection and Microbiology, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, China<i>Magnaporthe oryzae</i> (synonym <i>Pyricularia oryzae</i>) is a filamentous fungal pathogen that causes major yield losses in cultivated rice worldwide. However, the mechanisms of infection of <i>M. oryzae</i> are not well characterized. The VPS13 proteins play vital roles in various biological processes in many eukaryotic organisms, including in the organization of actin cytoskeleton, vesicle trafficking, mitochondrial fusion, and phagocytosis. Nevertheless, the function of the Vps13 protein in plant pathogenic fungi has not been explored. Here, we analysed the biological functions of the Vps13 protein in the development and pathogenicity of <i>M.</i> <i>oryzae</i>. Deletion mutants of MoVps13 significantly reduced the conidiation and decreased the rate of fungal infection on hosts. Moreover, the loss of MoVps13 resulted in defective cell wall integrity (CWI) and plasma membrane (PM) homeostasis when treated with chemicals for inducing cell wall stress (200 mg/mL Congo Red or 0.005% SDS) and sphingolipid synthesis inhibitors (2 μM myriocin or 2 μM amphotericin B). This indicated that MoVps13 is also involved in cell wall synthesis and sphingolipid synthesis. Through immunoblotting, autophagic flux detection, co-localization, and chemical drug sensitivity assays, we confirmed the involvement of Movps13 in ER-phagy and the response to ER stress. Additionally, we generated the C-terminal structure of MoVps13 with high accuracy using the alphaflod2 database. Our experimental evidence indicates that MoVps13 is an important virulence factor that regulates the pathogenicity of <i>M.</i> <i>oryzae</i> by controlling CWI, lipid metabolism and the ER-phagy pathway. These results have expanded our knowledge about pathogenic fungi and will help exploration for novel therapeutic strategies against the rice blast fungus.https://www.mdpi.com/2309-608X/7/12/1084<i>Magnaporthe</i> <i>oryzae</i>MoVps13ER-phagypathogenic fungicell wall integrity
spellingShingle Xueming Zhu
Lin Li
Jiaoyu Wang
Lili Zhao
Huanbin Shi
Jiandong Bao
Zhenzhu Su
Xiaohong Liu
Fucheng Lin
Vacuolar Protein-Sorting Receptor MoVps13 Regulates Conidiation and Pathogenicity in Rice Blast Fungus <i>Magnaporthe oryzae</i>
Journal of Fungi
<i>Magnaporthe</i> <i>oryzae</i>
MoVps13
ER-phagy
pathogenic fungi
cell wall integrity
title Vacuolar Protein-Sorting Receptor MoVps13 Regulates Conidiation and Pathogenicity in Rice Blast Fungus <i>Magnaporthe oryzae</i>
title_full Vacuolar Protein-Sorting Receptor MoVps13 Regulates Conidiation and Pathogenicity in Rice Blast Fungus <i>Magnaporthe oryzae</i>
title_fullStr Vacuolar Protein-Sorting Receptor MoVps13 Regulates Conidiation and Pathogenicity in Rice Blast Fungus <i>Magnaporthe oryzae</i>
title_full_unstemmed Vacuolar Protein-Sorting Receptor MoVps13 Regulates Conidiation and Pathogenicity in Rice Blast Fungus <i>Magnaporthe oryzae</i>
title_short Vacuolar Protein-Sorting Receptor MoVps13 Regulates Conidiation and Pathogenicity in Rice Blast Fungus <i>Magnaporthe oryzae</i>
title_sort vacuolar protein sorting receptor movps13 regulates conidiation and pathogenicity in rice blast fungus i magnaporthe oryzae i
topic <i>Magnaporthe</i> <i>oryzae</i>
MoVps13
ER-phagy
pathogenic fungi
cell wall integrity
url https://www.mdpi.com/2309-608X/7/12/1084
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