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Induced proximity of a TIR signaling domain on a plant-mammalian NLR chimera activates defense in plants.

Identifieur interne : 000131 ( Main/Exploration ); précédent : 000130; suivant : 000132

Induced proximity of a TIR signaling domain on a plant-mammalian NLR chimera activates defense in plants.

Auteurs : Zane Duxbury [Royaume-Uni] ; Shanshan Wang [Royaume-Uni] ; Craig I. Mackenzie [Royaume-Uni] ; Jeannette L. Tenthorey [États-Unis] ; Xiaoxiao Zhang [Australie] ; Sung Un Huh [Royaume-Uni, Corée du Sud] ; Lanxi Hu [Royaume-Uni] ; Lionel Hill [Royaume-Uni] ; Pok Man Ngou [Royaume-Uni] ; Pingtao Ding [Royaume-Uni] ; Jian Chen [Australie] ; Yan Ma [Royaume-Uni] ; Hailong Guo [Royaume-Uni] ; Baptiste Castel [Royaume-Uni] ; Panagiotis N. Moschou [Royaume-Uni, Suède, Grèce] ; Maud Bernoux [Australie] ; Peter N. Dodds [Australie] ; Russell E. Vance [États-Unis] ; Jonathan D G. Jones [Royaume-Uni]

Source :

RBID : pubmed:32709746

Descripteurs français

English descriptors

Abstract

Plant and animal intracellular nucleotide-binding, leucine-rich repeat (NLR) immune receptors detect pathogen-derived molecules and activate defense. Plant NLRs can be divided into several classes based upon their N-terminal signaling domains, including TIR (Toll-like, Interleukin-1 receptor, Resistance protein)- and CC (coiled-coil)-NLRs. Upon ligand detection, mammalian NAIP and NLRC4 NLRs oligomerize, forming an inflammasome that induces proximity of its N-terminal signaling domains. Recently, a plant CC-NLR was revealed to form an inflammasome-like hetero-oligomer. To further investigate plant NLR signaling mechanisms, we fused the N-terminal TIR domain of several plant NLRs to the N terminus of NLRC4. Inflammasome-dependent induced proximity of the TIR domain in planta initiated defense signaling. Thus, induced proximity of a plant TIR domain imposed by oligomerization of a mammalian inflammasome is sufficient to activate authentic plant defense. Ligand detection and inflammasome formation is maintained when the known components of the NLRC4 inflammasome is transferred across kingdoms, indicating that NLRC4 complex can robustly function without any additional mammalian proteins. Additionally, we found NADase activity of a plant TIR domain is necessary for plant defense activation, but NADase activity of a mammalian or a bacterial TIR is not sufficient to activate defense in plants.

DOI: 10.1073/pnas.2001185117
PubMed: 32709746
PubMed Central: PMC7414095


Affiliations:


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


Le document en format XML

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<nlm:affiliation>Department of Biology, University of Crete, GR 71 500 Heraklion, Crete, Greece.</nlm:affiliation>
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<name sortKey="Chen, Jian" sort="Chen, Jian" uniqKey="Chen J" first="Jian" last="Chen">Jian Chen</name>
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<name sortKey="Ma, Yan" sort="Ma, Yan" uniqKey="Ma Y" first="Yan" last="Ma">Yan Ma</name>
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<name sortKey="Moschou, Panagiotis N" sort="Moschou, Panagiotis N" uniqKey="Moschou P" first="Panagiotis N" last="Moschou">Panagiotis N. Moschou</name>
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<country xml:lang="fr">Suède</country>
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<name sortKey="Bernoux, Maud" sort="Bernoux, Maud" uniqKey="Bernoux M" first="Maud" last="Bernoux">Maud Bernoux</name>
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<name sortKey="Jones, Jonathan D G" sort="Jones, Jonathan D G" uniqKey="Jones J" first="Jonathan D G" last="Jones">Jonathan D G. Jones</name>
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<term>Animals (MeSH)</term>
<term>Inflammasomes (genetics)</term>
<term>Inflammasomes (immunology)</term>
<term>Inflammasomes (metabolism)</term>
<term>Mammals (MeSH)</term>
<term>NLR Proteins (chemistry)</term>
<term>NLR Proteins (genetics)</term>
<term>NLR Proteins (immunology)</term>
<term>NLR Proteins (metabolism)</term>
<term>Plant Immunity (genetics)</term>
<term>Plant Immunity (immunology)</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (immunology)</term>
<term>Plant Proteins (metabolism)</term>
<term>Protein Domains (genetics)</term>
<term>Protein Domains (physiology)</term>
<term>Recombinant Fusion Proteins (chemistry)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (immunology)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Signal Transduction (genetics)</term>
<term>Signal Transduction (immunology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Animaux (MeSH)</term>
<term>Domaines protéiques (génétique)</term>
<term>Domaines protéiques (physiologie)</term>
<term>Immunité des plantes (génétique)</term>
<term>Immunité des plantes (immunologie)</term>
<term>Inflammasomes (génétique)</term>
<term>Inflammasomes (immunologie)</term>
<term>Inflammasomes (métabolisme)</term>
<term>Mammifères (MeSH)</term>
<term>Protéines NLR (composition chimique)</term>
<term>Protéines NLR (génétique)</term>
<term>Protéines NLR (immunologie)</term>
<term>Protéines NLR (métabolisme)</term>
<term>Protéines de fusion recombinantes (composition chimique)</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (immunologie)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines végétales (composition chimique)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (immunologie)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Transduction du signal (génétique)</term>
<term>Transduction du signal (immunologie)</term>
</keywords>
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<term>NLR Proteins</term>
<term>Plant Proteins</term>
<term>Recombinant Fusion Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en">
<term>Inflammasomes</term>
<term>NLR Proteins</term>
<term>Plant Proteins</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en">
<term>Inflammasomes</term>
<term>NLR Proteins</term>
<term>Plant Proteins</term>
<term>Recombinant Fusion Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Inflammasomes</term>
<term>NLR Proteins</term>
<term>Plant Proteins</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
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<term>Protéines NLR</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines végétales</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Plant Immunity</term>
<term>Protein Domains</term>
<term>Signal Transduction</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Domaines protéiques</term>
<term>Immunité des plantes</term>
<term>Inflammasomes</term>
<term>Protéines NLR</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines végétales</term>
<term>Transduction du signal</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr">
<term>Immunité des plantes</term>
<term>Inflammasomes</term>
<term>Protéines NLR</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines végétales</term>
<term>Transduction du signal</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en">
<term>Plant Immunity</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Inflammasomes</term>
<term>Protéines NLR</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines végétales</term>
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<term>Domaines protéiques</term>
</keywords>
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<term>Protein Domains</term>
</keywords>
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<term>Animals</term>
<term>Mammals</term>
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<front>
<div type="abstract" xml:lang="en">Plant and animal intracellular nucleotide-binding, leucine-rich repeat (NLR) immune receptors detect pathogen-derived molecules and activate defense. Plant NLRs can be divided into several classes based upon their N-terminal signaling domains, including TIR (Toll-like, Interleukin-1 receptor, Resistance protein)- and CC (coiled-coil)-NLRs. Upon ligand detection, mammalian NAIP and NLRC4 NLRs oligomerize, forming an inflammasome that induces proximity of its N-terminal signaling domains. Recently, a plant CC-NLR was revealed to form an inflammasome-like hetero-oligomer. To further investigate plant NLR signaling mechanisms, we fused the N-terminal TIR domain of several plant NLRs to the N terminus of NLRC4. Inflammasome-dependent induced proximity of the TIR domain in planta initiated defense signaling. Thus, induced proximity of a plant TIR domain imposed by oligomerization of a mammalian inflammasome is sufficient to activate authentic plant defense. Ligand detection and inflammasome formation is maintained when the known components of the NLRC4 inflammasome is transferred across kingdoms, indicating that NLRC4 complex can robustly function without any additional mammalian proteins. Additionally, we found NADase activity of a plant TIR domain is necessary for plant defense activation, but NADase activity of a mammalian or a bacterial TIR is not sufficient to activate defense in plants.</div>
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<Year>2020</Year>
<Month>09</Month>
<Day>21</Day>
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<Year>2020</Year>
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<Day>04</Day>
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<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
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<ArticleTitle>Induced proximity of a TIR signaling domain on a plant-mammalian NLR chimera activates defense in plants.</ArticleTitle>
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<AbstractText>Plant and animal intracellular nucleotide-binding, leucine-rich repeat (NLR) immune receptors detect pathogen-derived molecules and activate defense. Plant NLRs can be divided into several classes based upon their N-terminal signaling domains, including TIR (Toll-like, Interleukin-1 receptor, Resistance protein)- and CC (coiled-coil)-NLRs. Upon ligand detection, mammalian NAIP and NLRC4 NLRs oligomerize, forming an inflammasome that induces proximity of its N-terminal signaling domains. Recently, a plant CC-NLR was revealed to form an inflammasome-like hetero-oligomer. To further investigate plant NLR signaling mechanisms, we fused the N-terminal TIR domain of several plant NLRs to the N terminus of NLRC4. Inflammasome-dependent induced proximity of the TIR domain in planta initiated defense signaling. Thus, induced proximity of a plant TIR domain imposed by oligomerization of a mammalian inflammasome is sufficient to activate authentic plant defense. Ligand detection and inflammasome formation is maintained when the known components of the NLRC4 inflammasome is transferred across kingdoms, indicating that NLRC4 complex can robustly function without any additional mammalian proteins. Additionally, we found NADase activity of a plant TIR domain is necessary for plant defense activation, but NADase activity of a mammalian or a bacterial TIR is not sufficient to activate defense in plants.</AbstractText>
<CopyrightInformation>Copyright © 2020 the Author(s). Published by PNAS.</CopyrightInformation>
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<AffiliationInfo>
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