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Phytophthora infestans RXLR effector SFI5 requires association with calmodulin for PTI/MTI suppressing activity.

Identifieur interne : 000701 ( Main/Exploration ); précédent : 000700; suivant : 000702

Phytophthora infestans RXLR effector SFI5 requires association with calmodulin for PTI/MTI suppressing activity.

Auteurs : Xiangzi Zheng [Allemagne, République populaire de Chine] ; Nadine Wagener [Allemagne] ; Hazel Mclellan [Royaume-Uni] ; Petra C. Boevink [Royaume-Uni] ; Chenlei Hua [Allemagne] ; Paul R J. Birch [Royaume-Uni] ; Frédéric Brunner [Allemagne, Espagne]

Source :

RBID : pubmed:29932222

Descripteurs français

English descriptors

Abstract

Pathogens secrete effector proteins to interfere with plant innate immunity, in which Ca2+ /calmodulin (CaM) signalling plays key roles. Thus far, few effectors have been identified that directly interact with CaM for defence suppression. Here, we report that SFI5, an RXLR effector from Phytophthora infestans, suppresses microbe-associated molecular pattern (MAMP)-triggered immunity (MTI) by interacting with host CaMs. We predicted the CaM-binding site in SFI5 using in silico analysis. The interaction between SFI5 and CaM was tested by both in vitro and in vivo assays. MTI suppression by SFI5 and truncated variants were performed in a tomato protoplast system. We found that both the predicted CaM-binding site and the full-length SFI5 protein interact with CaM in the presence of Ca2+ . MTI responses, such as FRK1 upregulation, reactive oxygen species accumulation, and mitogen-activated protein kinase activation were suppressed by truncated SFI5 proteins containing the C-terminal CaM-binding site but not by those without it. The plasma membrane localization of SFI5 and its ability to enhance infection were also perturbed by loss of the CaM-binding site. We conclude that CaM-binding is required for localization and activity of SFI5. We propose that SFI5 suppresses plant immunity by interfering with immune signalling components after activation by CaMs.

DOI: 10.1111/nph.15250
PubMed: 29932222
PubMed Central: PMC6099356


Affiliations:


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Le document en format XML

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<term>Amino Acid Motifs (MeSH)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Calcium (pharmacology)</term>
<term>Calmodulin (metabolism)</term>
<term>Cell Membrane (metabolism)</term>
<term>Lycopersicon esculentum (immunology)</term>
<term>Lycopersicon esculentum (metabolism)</term>
<term>Lycopersicon esculentum (microbiology)</term>
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<term>Calmoduline (métabolisme)</term>
<term>Immunité des plantes (effets des médicaments et des substances chimiques)</term>
<term>Liaison aux protéines (effets des médicaments et des substances chimiques)</term>
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<term>Lycopersicon esculentum (microbiologie)</term>
<term>Lycopersicon esculentum (métabolisme)</term>
<term>Membrane cellulaire (métabolisme)</term>
<term>Molécules contenant des motifs associés aux pathogènes (métabolisme)</term>
<term>Motifs d'acides aminés (MeSH)</term>
<term>Peptides (composition chimique)</term>
<term>Peptides (métabolisme)</term>
<term>Phytophthora infestans (effets des médicaments et des substances chimiques)</term>
<term>Phytophthora infestans (métabolisme)</term>
<term>Protéines (composition chimique)</term>
<term>Protéines (métabolisme)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<term>Proteins</term>
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<term>Peptides</term>
<term>Protéines</term>
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<keywords scheme="MESH" qualifier="drug effects" xml:lang="en">
<term>Phytophthora infestans</term>
<term>Plant Immunity</term>
<term>Protein Binding</term>
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<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr">
<term>Immunité des plantes</term>
<term>Liaison aux protéines</term>
<term>Phytophthora infestans</term>
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<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr">
<term>Lycopersicon esculentum</term>
</keywords>
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<term>Lycopersicon esculentum</term>
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<term>Cell Membrane</term>
<term>Lycopersicon esculentum</term>
<term>Phytophthora infestans</term>
</keywords>
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<term>Lycopersicon esculentum</term>
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<term>Lycopersicon esculentum</term>
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<term>Calmoduline</term>
<term>Lycopersicon esculentum</term>
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<term>Phytophthora infestans</term>
<term>Protéines</term>
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<term>Amino Acid Sequence</term>
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<term>Motifs d'acides aminés</term>
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<div type="abstract" xml:lang="en">Pathogens secrete effector proteins to interfere with plant innate immunity, in which Ca
<sup>2+</sup>
/calmodulin (CaM) signalling plays key roles. Thus far, few effectors have been identified that directly interact with CaM for defence suppression. Here, we report that SFI5, an RXLR effector from Phytophthora infestans, suppresses microbe-associated molecular pattern (MAMP)-triggered immunity (MTI) by interacting with host CaMs. We predicted the CaM-binding site in SFI5 using in silico analysis. The interaction between SFI5 and CaM was tested by both in vitro and in vivo assays. MTI suppression by SFI5 and truncated variants were performed in a tomato protoplast system. We found that both the predicted CaM-binding site and the full-length SFI5 protein interact with CaM in the presence of Ca
<sup>2+</sup>
. MTI responses, such as FRK1 upregulation, reactive oxygen species accumulation, and mitogen-activated protein kinase activation were suppressed by truncated SFI5 proteins containing the C-terminal CaM-binding site but not by those without it. The plasma membrane localization of SFI5 and its ability to enhance infection were also perturbed by loss of the CaM-binding site. We conclude that CaM-binding is required for localization and activity of SFI5. We propose that SFI5 suppresses plant immunity by interfering with immune signalling components after activation by CaMs.</div>
</front>
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<AbstractText>Pathogens secrete effector proteins to interfere with plant innate immunity, in which Ca
<sup>2+</sup>
/calmodulin (CaM) signalling plays key roles. Thus far, few effectors have been identified that directly interact with CaM for defence suppression. Here, we report that SFI5, an RXLR effector from Phytophthora infestans, suppresses microbe-associated molecular pattern (MAMP)-triggered immunity (MTI) by interacting with host CaMs. We predicted the CaM-binding site in SFI5 using in silico analysis. The interaction between SFI5 and CaM was tested by both in vitro and in vivo assays. MTI suppression by SFI5 and truncated variants were performed in a tomato protoplast system. We found that both the predicted CaM-binding site and the full-length SFI5 protein interact with CaM in the presence of Ca
<sup>2+</sup>
. MTI responses, such as FRK1 upregulation, reactive oxygen species accumulation, and mitogen-activated protein kinase activation were suppressed by truncated SFI5 proteins containing the C-terminal CaM-binding site but not by those without it. The plasma membrane localization of SFI5 and its ability to enhance infection were also perturbed by loss of the CaM-binding site. We conclude that CaM-binding is required for localization and activity of SFI5. We propose that SFI5 suppresses plant immunity by interfering with immune signalling components after activation by CaMs.</AbstractText>
<CopyrightInformation>© 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y">
<Author ValidYN="Y">
<LastName>Zheng</LastName>
<ForeName>Xiangzi</ForeName>
<Initials>X</Initials>
<AffiliationInfo>
<Affiliation>Department of Biochemistry, Centre for Plant Molecular Biology, Eberhard Karls University, Auf der Morgenstelle 32, D-72076, Tübingen, Germany.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Center for Molecular Cell and Systems Biology, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou, 350002, China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y">
<LastName>Wagener</LastName>
<ForeName>Nadine</ForeName>
<Initials>N</Initials>
<AffiliationInfo>
<Affiliation>Department of Biochemistry, Centre for Plant Molecular Biology, Eberhard Karls University, Auf der Morgenstelle 32, D-72076, Tübingen, Germany.</Affiliation>
</AffiliationInfo>
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<LastName>McLellan</LastName>
<ForeName>Hazel</ForeName>
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<Identifier Source="ORCID">0000-0003-4490-7053</Identifier>
<AffiliationInfo>
<Affiliation>Division of Plant Sciences, University of Dundee (at James Hutton Institute), Errol Rd, Invergowrie, Dundee, DD2 5DA, UK.</Affiliation>
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<ForeName>Petra C</ForeName>
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<Affiliation>Cell and Molecular Sciences, The James Hutton Institute, Errol Rd, Invergowrie, Dundee, DD2 5DA, UK.</Affiliation>
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<LastName>Hua</LastName>
<ForeName>Chenlei</ForeName>
<Initials>C</Initials>
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<Affiliation>Department of Biochemistry, Centre for Plant Molecular Biology, Eberhard Karls University, Auf der Morgenstelle 32, D-72076, Tübingen, Germany.</Affiliation>
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<ForeName>Paul R J</ForeName>
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<Affiliation>Division of Plant Sciences, University of Dundee (at James Hutton Institute), Errol Rd, Invergowrie, Dundee, DD2 5DA, UK.</Affiliation>
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<ForeName>Frédéric</ForeName>
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<AffiliationInfo>
<Affiliation>Department of Biochemistry, Centre for Plant Molecular Biology, Eberhard Karls University, Auf der Morgenstelle 32, D-72076, Tübingen, Germany.</Affiliation>
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<Affiliation>PlantResponse Biotech, S.L., Centre for Plant Biotechnology and Genomics (CBGP), Campus de Montegancedo, 28223, Pozuelo de Alarcón, Madrid, Spain.</Affiliation>
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<name sortKey="Wagener, Nadine" sort="Wagener, Nadine" uniqKey="Wagener N" first="Nadine" last="Wagener">Nadine Wagener</name>
</country>
<country name="République populaire de Chine">
<noRegion>
<name sortKey="Zheng, Xiangzi" sort="Zheng, Xiangzi" uniqKey="Zheng X" first="Xiangzi" last="Zheng">Xiangzi Zheng</name>
</noRegion>
</country>
<country name="Royaume-Uni">
<noRegion>
<name sortKey="Mclellan, Hazel" sort="Mclellan, Hazel" uniqKey="Mclellan H" first="Hazel" last="Mclellan">Hazel Mclellan</name>
</noRegion>
<name sortKey="Birch, Paul R J" sort="Birch, Paul R J" uniqKey="Birch P" first="Paul R J" last="Birch">Paul R J. Birch</name>
<name sortKey="Birch, Paul R J" sort="Birch, Paul R J" uniqKey="Birch P" first="Paul R J" last="Birch">Paul R J. Birch</name>
<name sortKey="Boevink, Petra C" sort="Boevink, Petra C" uniqKey="Boevink P" first="Petra C" last="Boevink">Petra C. Boevink</name>
</country>
<country name="Espagne">
<region name="Communauté de Madrid">
<name sortKey="Brunner, Frederic" sort="Brunner, Frederic" uniqKey="Brunner F" first="Frédéric" last="Brunner">Frédéric Brunner</name>
</region>
</country>
</tree>
</affiliations>
</record>

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   |texte=   Phytophthora infestans RXLR effector SFI5 requires association with calmodulin for PTI/MTI suppressing activity.
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