PlantImRecepV1, Main, Exploration, bibRecord, 000233

A fungal effector and a rice NLR protein have antagonistic effects on a Bowman-Birk trypsin inhibitor.

Identifieur interne : 000233 ( Main/Exploration ); précédent : 000232; suivant : 000234

A fungal effector and a rice NLR protein have antagonistic effects on a Bowman-Birk trypsin inhibitor.

Source :

Plant biotechnology journal [ 1467-7652 ] ; 2020.

RBID : pubmed:32415911

Descripteurs français

KwdFr :
- Inhibiteurs trypsiques (MeSH), Magnaporthe (MeSH), Maladies des plantes (MeSH), Oryza (génétique), Protéines NLR (MeSH), Protéines végétales (génétique).
MESH :
- génétique : Oryza, Protéines végétales.
- Inhibiteurs trypsiques, Magnaporthe, Maladies des plantes, Protéines NLR.

English descriptors

KwdEn :
- Magnaporthe (MeSH), NLR Proteins (MeSH), Oryza (genetics), Plant Diseases (MeSH), Plant Proteins (genetics), Trypsin Inhibitors (MeSH).
MESH :
- chemical , genetics : Plant Proteins.
- chemical : NLR Proteins, Trypsin Inhibitors.
- genetics : Oryza.
- Magnaporthe, Plant Diseases.

Abstract

Bowman-Birk trypsin inhibitors (BBIs) play important roles in animal and plant immunity, but how these protease inhibitors are involved in the immune system remains unclear. Here, we show that the rice (Oryza sativa) BBI protein APIP4 is a common target of a fungal effector and an NLR receptor for innate immunity. APIP4 exhibited trypsin inhibitor activity in vitro and in vivo. Knockout of APIP4 in rice enhanced susceptibility, and overexpression of APIP4 increased resistance to the fungal pathogen Magnaporthe oryzae. The M. oryzae effector AvrPiz-t interacted with APIP4 and suppressed APIP4 trypsin inhibitor activity. By contrast, the rice NLR protein Piz-t interacted with APIP4, enhancing APIP4 transcript and protein levels, and protease inhibitor activity. Our findings reveal a novel host defence mechanism in which a host protease inhibitor targeted by a fungal pathogen is protected by an NLR receptor.

DOI: 10.1111/pbi.13400
PubMed: 32415911
PubMed Central: PMC7589341

Affiliations:

République populaire de Chine, États-Unis

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000129
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Le document en format XML

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<author><name sortKey="Wang, Jiyang" sort="Wang, Jiyang" uniqKey="Wang J" first="Jiyang" last="Wang">Jiyang Wang</name>
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<country xml:lang="fr">République populaire de Chine</country>
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<author><name sortKey="Park, Chan Ho" sort="Park, Chan Ho" uniqKey="Park C" first="Chan-Ho" last="Park">Chan-Ho Park</name>
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<author><name sortKey="Bellizzi, Maria" sort="Bellizzi, Maria" uniqKey="Bellizzi M" first="Maria" last="Bellizzi">Maria Bellizzi</name>
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<author><name sortKey="Zhou, Xueping" sort="Zhou, Xueping" uniqKey="Zhou X" first="Xueping" last="Zhou">Xueping Zhou</name>
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<author><name sortKey="Ning, Yuese" sort="Ning, Yuese" uniqKey="Ning Y" first="Yuese" last="Ning">Yuese Ning</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Magnaporthe (MeSH)</term>
<term>NLR Proteins (MeSH)</term>
<term>Oryza (genetics)</term>
<term>Plant Diseases (MeSH)</term>
<term>Plant Proteins (genetics)</term>
<term>Trypsin Inhibitors (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Inhibiteurs trypsiques (MeSH)</term>
<term>Magnaporthe (MeSH)</term>
<term>Maladies des plantes (MeSH)</term>
<term>Oryza (génétique)</term>
<term>Protéines NLR (MeSH)</term>
<term>Protéines végétales (génétique)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>NLR Proteins</term>
<term>Trypsin Inhibitors</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Oryza</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Oryza</term>
<term>Protéines végétales</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Magnaporthe</term>
<term>Plant Diseases</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Inhibiteurs trypsiques</term>
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<front><div type="abstract" xml:lang="en">Bowman-Birk trypsin inhibitors (BBIs) play important roles in animal and plant immunity, but how these protease inhibitors are involved in the immune system remains unclear. Here, we show that the rice (Oryza sativa) BBI protein APIP4 is a common target of a fungal effector and an NLR receptor for innate immunity. APIP4 exhibited trypsin inhibitor activity in vitro and in vivo. Knockout of APIP4 in rice enhanced susceptibility, and overexpression of APIP4 increased resistance to the fungal pathogen Magnaporthe oryzae. The M. oryzae effector AvrPiz-t interacted with APIP4 and suppressed APIP4 trypsin inhibitor activity. By contrast, the rice NLR protein Piz-t interacted with APIP4, enhancing APIP4 transcript and protein levels, and protease inhibitor activity. Our findings reveal a novel host defence mechanism in which a host protease inhibitor targeted by a fungal pathogen is protected by an NLR receptor.</div>
</front>
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<Abstract><AbstractText>Bowman-Birk trypsin inhibitors (BBIs) play important roles in animal and plant immunity, but how these protease inhibitors are involved in the immune system remains unclear. Here, we show that the rice (Oryza sativa) BBI protein APIP4 is a common target of a fungal effector and an NLR receptor for innate immunity. APIP4 exhibited trypsin inhibitor activity in vitro and in vivo. Knockout of APIP4 in rice enhanced susceptibility, and overexpression of APIP4 increased resistance to the fungal pathogen Magnaporthe oryzae. The M. oryzae effector AvrPiz-t interacted with APIP4 and suppressed APIP4 trypsin inhibitor activity. By contrast, the rice NLR protein Piz-t interacted with APIP4, enhancing APIP4 transcript and protein levels, and protease inhibitor activity. Our findings reveal a novel host defence mechanism in which a host protease inhibitor targeted by a fungal pathogen is protected by an NLR receptor.</AbstractText>
<CopyrightInformation>© 2020 The Authors. Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Chongyang</ForeName>
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<AffiliationInfo><Affiliation>State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, 100193, China.</Affiliation>
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<AffiliationInfo><Affiliation>Department of Plant Pathology, Ohio State University, Columbus, OH, 43210, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Fang</LastName>
<ForeName>Hong</ForeName>
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<Author ValidYN="Y"><LastName>Shi</LastName>
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	Serveur d'exploration sur les récepteurs immunitaires végétaux
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Serveur d'exploration sur les récepteurs immunitaires végétaux

A fungal effector and a rice NLR protein have antagonistic effects on a Bowman-Birk trypsin inhibitor.

A fungal effector and a rice NLR protein have antagonistic effects on a Bowman-Birk trypsin inhibitor.

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