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Tomato I2 Immune Receptor Can Be Engineered to Confer Partial Resistance to the Oomycete Phytophthora infestans in Addition to the Fungus Fusarium oxysporum.

Identifieur interne : 000D49 ( Main/Exploration ); précédent : 000D48; suivant : 000D50

Tomato I2 Immune Receptor Can Be Engineered to Confer Partial Resistance to the Oomycete Phytophthora infestans in Addition to the Fungus Fusarium oxysporum.

Auteurs : Artemis Giannakopoulou [Royaume-Uni] ; John F C. Steele [Royaume-Uni] ; Maria Eugenia Segretin [Argentine] ; Tolga O. Bozkurt [Royaume-Uni] ; Ji Zhou [Royaume-Uni] ; Silke Robatzek [Royaume-Uni] ; Mark J. Banfield [Royaume-Uni] ; Marina Pais [Royaume-Uni] ; Sophien Kamoun [Royaume-Uni]

Source :

RBID : pubmed:26367241

Descripteurs français

English descriptors

Abstract

Plants and animals rely on immune receptors, known as nucleotide-binding domain and leucine-rich repeat (NLR)-containing proteins, to defend against invading pathogens and activate immune responses. How NLR receptors respond to pathogens is inadequately understood. We previously reported single-residue mutations that expand the response of the potato immune receptor R3a to AVR3a(EM), a stealthy effector from the late blight oomycete pathogen Phytophthora infestans. I2, another NLR that mediates resistance to the will-causing fungus Fusarium oxysporum f. sp. lycopersici, is the tomato ortholog of R3a. We transferred previously identified R3a mutations to I2 to assess the degree to which the resulting I2 mutants have an altered response. We discovered that wild-type I2 protein responds weakly to AVR3a. One mutant in the N-terminal coiled-coil domain, I2(I141N), appeared sensitized and displayed markedly increased response to AVR3a. Remarkably, I2(I141N) conferred partial resistance to P. infestans. Further, I2(I141N) has an expanded response spectrum to F. oxysporum f. sp. lycopersici effectors compared with the wild-type I2 protein. Our results suggest that synthetic immune receptors can be engineered to confer resistance to phylogenetically divergent pathogens and indicate that knowledge gathered for one NLR could be exploited to improve NLR from other plant species.

DOI: 10.1094/MPMI-07-15-0147-R
PubMed: 26367241


Affiliations:


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Le document en format XML

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<term>Amino Acid Sequence (MeSH)</term>
<term>Fusarium (immunology)</term>
<term>Fusarium (pathogenicity)</term>
<term>Lycopersicon esculentum (immunology)</term>
<term>Lycopersicon esculentum (microbiology)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Phytophthora infestans (immunology)</term>
<term>Phytophthora infestans (pathogenicity)</term>
<term>Receptors, Immunologic (chemistry)</term>
<term>Receptors, Immunologic (immunology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Données de séquences moléculaires (MeSH)</term>
<term>Fusarium (immunologie)</term>
<term>Fusarium (pathogénicité)</term>
<term>Lycopersicon esculentum (immunologie)</term>
<term>Lycopersicon esculentum (microbiologie)</term>
<term>Phytophthora infestans (immunologie)</term>
<term>Phytophthora infestans (pathogénicité)</term>
<term>Récepteurs immunologiques (composition chimique)</term>
<term>Récepteurs immunologiques (immunologie)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en">
<term>Receptors, Immunologic</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr">
<term>Récepteurs immunologiques</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr">
<term>Fusarium</term>
<term>Lycopersicon esculentum</term>
<term>Phytophthora infestans</term>
<term>Récepteurs immunologiques</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en">
<term>Fusarium</term>
<term>Lycopersicon esculentum</term>
<term>Phytophthora infestans</term>
<term>Receptors, Immunologic</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr">
<term>Lycopersicon esculentum</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en">
<term>Lycopersicon esculentum</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en">
<term>Fusarium</term>
<term>Phytophthora infestans</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr">
<term>Fusarium</term>
<term>Phytophthora infestans</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Amino Acid Sequence</term>
<term>Molecular Sequence Data</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr">
<term>Données de séquences moléculaires</term>
<term>Séquence d'acides aminés</term>
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<div type="abstract" xml:lang="en">Plants and animals rely on immune receptors, known as nucleotide-binding domain and leucine-rich repeat (NLR)-containing proteins, to defend against invading pathogens and activate immune responses. How NLR receptors respond to pathogens is inadequately understood. We previously reported single-residue mutations that expand the response of the potato immune receptor R3a to AVR3a(EM), a stealthy effector from the late blight oomycete pathogen Phytophthora infestans. I2, another NLR that mediates resistance to the will-causing fungus Fusarium oxysporum f. sp. lycopersici, is the tomato ortholog of R3a. We transferred previously identified R3a mutations to I2 to assess the degree to which the resulting I2 mutants have an altered response. We discovered that wild-type I2 protein responds weakly to AVR3a. One mutant in the N-terminal coiled-coil domain, I2(I141N), appeared sensitized and displayed markedly increased response to AVR3a. Remarkably, I2(I141N) conferred partial resistance to P. infestans. Further, I2(I141N) has an expanded response spectrum to F. oxysporum f. sp. lycopersici effectors compared with the wild-type I2 protein. Our results suggest that synthetic immune receptors can be engineered to confer resistance to phylogenetically divergent pathogens and indicate that knowledge gathered for one NLR could be exploited to improve NLR from other plant species.</div>
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<AbstractText>Plants and animals rely on immune receptors, known as nucleotide-binding domain and leucine-rich repeat (NLR)-containing proteins, to defend against invading pathogens and activate immune responses. How NLR receptors respond to pathogens is inadequately understood. We previously reported single-residue mutations that expand the response of the potato immune receptor R3a to AVR3a(EM), a stealthy effector from the late blight oomycete pathogen Phytophthora infestans. I2, another NLR that mediates resistance to the will-causing fungus Fusarium oxysporum f. sp. lycopersici, is the tomato ortholog of R3a. We transferred previously identified R3a mutations to I2 to assess the degree to which the resulting I2 mutants have an altered response. We discovered that wild-type I2 protein responds weakly to AVR3a. One mutant in the N-terminal coiled-coil domain, I2(I141N), appeared sensitized and displayed markedly increased response to AVR3a. Remarkably, I2(I141N) conferred partial resistance to P. infestans. Further, I2(I141N) has an expanded response spectrum to F. oxysporum f. sp. lycopersici effectors compared with the wild-type I2 protein. Our results suggest that synthetic immune receptors can be engineered to confer resistance to phylogenetically divergent pathogens and indicate that knowledge gathered for one NLR could be exploited to improve NLR from other plant species.</AbstractText>
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</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y">
<Grant>
<GrantID>BBS/E/J/000C0624</GrantID>
<Agency>Biotechnology and Biological Sciences Research Council</Agency>
<Country>United Kingdom</Country>
</Grant>
</GrantList>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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<ArticleDate DateType="Electronic">
<Year>2015</Year>
<Month>12</Month>
<Day>04</Day>
</ArticleDate>
</Article>
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<Country>United States</Country>
<MedlineTA>Mol Plant Microbe Interact</MedlineTA>
<NlmUniqueID>9107902</NlmUniqueID>
<ISSNLinking>0894-0282</ISSNLinking>
</MedlineJournalInfo>
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<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011971">Receptors, Immunologic</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList>
<MeshHeading>
<DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D005670" MajorTopicYN="N">Fusarium</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
<QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D018551" MajorTopicYN="N">Lycopersicon esculentum</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D055750" MajorTopicYN="N">Phytophthora infestans</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
<QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D011971" MajorTopicYN="N">Receptors, Immunologic</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
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<PubMedPubDate PubStatus="entrez">
<Year>2015</Year>
<Month>9</Month>
<Day>15</Day>
<Hour>6</Hour>
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<PubMedPubDate PubStatus="pubmed">
<Year>2015</Year>
<Month>9</Month>
<Day>15</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline">
<Year>2016</Year>
<Month>2</Month>
<Day>10</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList>
<ArticleId IdType="pubmed">26367241</ArticleId>
<ArticleId IdType="doi">10.1094/MPMI-07-15-0147-R</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations>
<list>
<country>
<li>Argentine</li>
<li>Royaume-Uni</li>
</country>
</list>
<tree>
<country name="Royaume-Uni">
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<name sortKey="Giannakopoulou, Artemis" sort="Giannakopoulou, Artemis" uniqKey="Giannakopoulou A" first="Artemis" last="Giannakopoulou">Artemis Giannakopoulou</name>
</noRegion>
<name sortKey="Banfield, Mark J" sort="Banfield, Mark J" uniqKey="Banfield M" first="Mark J" last="Banfield">Mark J. Banfield</name>
<name sortKey="Bozkurt, Tolga O" sort="Bozkurt, Tolga O" uniqKey="Bozkurt T" first="Tolga O" last="Bozkurt">Tolga O. Bozkurt</name>
<name sortKey="Kamoun, Sophien" sort="Kamoun, Sophien" uniqKey="Kamoun S" first="Sophien" last="Kamoun">Sophien Kamoun</name>
<name sortKey="Pais, Marina" sort="Pais, Marina" uniqKey="Pais M" first="Marina" last="Pais">Marina Pais</name>
<name sortKey="Robatzek, Silke" sort="Robatzek, Silke" uniqKey="Robatzek S" first="Silke" last="Robatzek">Silke Robatzek</name>
<name sortKey="Steele, John F C" sort="Steele, John F C" uniqKey="Steele J" first="John F C" last="Steele">John F C. Steele</name>
<name sortKey="Zhou, Ji" sort="Zhou, Ji" uniqKey="Zhou J" first="Ji" last="Zhou">Ji Zhou</name>
<name sortKey="Zhou, Ji" sort="Zhou, Ji" uniqKey="Zhou J" first="Ji" last="Zhou">Ji Zhou</name>
</country>
<country name="Argentine">
<noRegion>
<name sortKey="Segretin, Maria Eugenia" sort="Segretin, Maria Eugenia" uniqKey="Segretin M" first="Maria Eugenia" last="Segretin">Maria Eugenia Segretin</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

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