An effector-targeted protease contributes to defense against Phytophthora infestans and is under diversifying selection in natural hosts.
Identifieur interne : 001983 ( Main/Exploration ); précédent : 001982; suivant : 001984An effector-targeted protease contributes to defense against Phytophthora infestans and is under diversifying selection in natural hosts.
Auteurs : Farnusch Kaschani [Allemagne] ; Mohammed Shabab ; Tolga Bozkurt ; Takayuki Shindo ; Sebastian Schornack ; Christian Gu ; Muhammad Ilyas ; Joe Win ; Sophien Kamoun ; Renier A L. Van Der HoornSource :
- Plant physiology [ 1532-2548 ] ; 2010.
Descripteurs français
- KwdFr :
- ADN des plantes (MeSH), Données de séquences moléculaires (MeSH), Extinction de l'expression des gènes (MeSH), Peptide hydrolases (génétique), Peptide hydrolases (métabolisme), Phylogenèse (MeSH), Phytophthora infestans (pathogénicité), RT-PCR (MeSH), Solanum (enzymologie), Solanum (microbiologie), Séquence nucléotidique (MeSH), Technique de Western (MeSH).
- MESH :
- enzymologie : Solanum.
- génétique : Peptide hydrolases.
- microbiologie : Solanum.
- métabolisme : Peptide hydrolases.
- pathogénicité : Phytophthora infestans.
- ADN des plantes, Données de séquences moléculaires, Extinction de l'expression des gènes, Phylogenèse, RT-PCR, Séquence nucléotidique, Technique de Western.
English descriptors
- KwdEn :
- Base Sequence (MeSH), Blotting, Western (MeSH), DNA, Plant (MeSH), Gene Silencing (MeSH), Molecular Sequence Data (MeSH), Peptide Hydrolases (genetics), Peptide Hydrolases (metabolism), Phylogeny (MeSH), Phytophthora infestans (pathogenicity), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Solanum (enzymology), Solanum (microbiology).
- MESH :
- chemical , genetics : Peptide Hydrolases.
- chemical , metabolism : Peptide Hydrolases.
- chemical : DNA, Plant.
- enzymology : Solanum.
- microbiology : Solanum.
- pathogenicity : Phytophthora infestans.
- Base Sequence, Blotting, Western, Gene Silencing, Molecular Sequence Data, Phylogeny, Reverse Transcriptase Polymerase Chain Reaction.
Abstract
Since the leaf apoplast is a primary habitat for many plant pathogens, apoplastic proteins are potent, ancient targets for apoplastic effectors secreted by plant pathogens. So far, however, only a few apoplastic effector targets have been identified and characterized. Here, we discovered that the papain-like cysteine protease C14 is a new common target of EPIC1 and EPIC2B, two apoplastic, cystatin-like proteins secreted by the potato (Solanum tuberosum) late blight pathogen Phytophthora infestans. C14 is a secreted protease of tomato (Solanum lycopersicum) and potato typified by a carboxyl-terminal granulin domain. The EPIC-C14 interaction occurs at a wide pH range and is stronger than the previously described interactions of EPICs with tomato defense proteases PIP1 and RCR3. The selectivity of the EPICs is also different when compared with the AVR2 effector of the fungal tomato pathogen Cladosporium fulvum, which targets PIP1 and RCR3, and only at apoplastic pH. Importantly, silencing of C14 increased susceptibility to P. infestans, demonstrating that this protease plays a role in pathogen defense. Although C14 is under conservative selection in tomato, it is under diversifying selection in wild potato species (Solanum demissum, Solanum verrucosum, and Solanum stoliniferum) that are the natural hosts of P. infestans. These data reveal a novel effector target in the apoplast that contributes to immunity and is under diversifying selection, but only in the natural host of the pathogen.
DOI: 10.1104/pp.110.158030
PubMed: 20940351
PubMed Central: PMC2996022
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Van Der Hoorn</name></author></analytic><series><title level="j">Plant physiology</title><idno type="eISSN">1532-2548</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence (MeSH)</term><term>Blotting, Western (MeSH)</term><term>DNA, Plant (MeSH)</term><term>Gene Silencing (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Peptide Hydrolases (genetics)</term><term>Peptide Hydrolases (metabolism)</term><term>Phylogeny (MeSH)</term><term>Phytophthora infestans (pathogenicity)</term><term>Reverse Transcriptase Polymerase Chain Reaction (MeSH)</term><term>Solanum (enzymology)</term><term>Solanum (microbiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN des plantes (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Extinction de l'expression des gènes (MeSH)</term><term>Peptide hydrolases (génétique)</term><term>Peptide hydrolases (métabolisme)</term><term>Phylogenèse (MeSH)</term><term>Phytophthora infestans (pathogénicité)</term><term>RT-PCR (MeSH)</term><term>Solanum (enzymologie)</term><term>Solanum (microbiologie)</term><term>Séquence nucléotidique (MeSH)</term><term>Technique de Western (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peptide Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>DNA, Plant</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Solanum</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Solanum</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peptide hydrolases</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Solanum</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Solanum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peptide hydrolases</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Phytophthora infestans</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Phytophthora infestans</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Blotting, Western</term><term>Gene Silencing</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Reverse Transcriptase Polymerase Chain Reaction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN des plantes</term><term>Données de séquences moléculaires</term><term>Extinction de l'expression des gènes</term><term>Phylogenèse</term><term>RT-PCR</term><term>Séquence nucléotidique</term><term>Technique de Western</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Since the leaf apoplast is a primary habitat for many plant pathogens, apoplastic proteins are potent, ancient targets for apoplastic effectors secreted by plant pathogens. So far, however, only a few apoplastic effector targets have been identified and characterized. Here, we discovered that the papain-like cysteine protease C14 is a new common target of EPIC1 and EPIC2B, two apoplastic, cystatin-like proteins secreted by the potato (Solanum tuberosum) late blight pathogen Phytophthora infestans. C14 is a secreted protease of tomato (Solanum lycopersicum) and potato typified by a carboxyl-terminal granulin domain. The EPIC-C14 interaction occurs at a wide pH range and is stronger than the previously described interactions of EPICs with tomato defense proteases PIP1 and RCR3. The selectivity of the EPICs is also different when compared with the AVR2 effector of the fungal tomato pathogen Cladosporium fulvum, which targets PIP1 and RCR3, and only at apoplastic pH. Importantly, silencing of C14 increased susceptibility to P. infestans, demonstrating that this protease plays a role in pathogen defense. Although C14 is under conservative selection in tomato, it is under diversifying selection in wild potato species (Solanum demissum, Solanum verrucosum, and Solanum stoliniferum) that are the natural hosts of P. infestans. These data reveal a novel effector target in the apoplast that contributes to immunity and is under diversifying selection, but only in the natural host of the pathogen.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20940351</PMID><DateCompleted><Year>2011</Year><Month>06</Month><Day>02</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1532-2548</ISSN><JournalIssue CitedMedium="Internet"><Volume>154</Volume><Issue>4</Issue><PubDate><Year>2010</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>An effector-targeted protease contributes to defense against Phytophthora infestans and is under diversifying selection in natural hosts.</ArticleTitle><Pagination><MedlinePgn>1794-804</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1104/pp.110.158030</ELocationID><Abstract><AbstractText>Since the leaf apoplast is a primary habitat for many plant pathogens, apoplastic proteins are potent, ancient targets for apoplastic effectors secreted by plant pathogens. So far, however, only a few apoplastic effector targets have been identified and characterized. Here, we discovered that the papain-like cysteine protease C14 is a new common target of EPIC1 and EPIC2B, two apoplastic, cystatin-like proteins secreted by the potato (Solanum tuberosum) late blight pathogen Phytophthora infestans. C14 is a secreted protease of tomato (Solanum lycopersicum) and potato typified by a carboxyl-terminal granulin domain. The EPIC-C14 interaction occurs at a wide pH range and is stronger than the previously described interactions of EPICs with tomato defense proteases PIP1 and RCR3. The selectivity of the EPICs is also different when compared with the AVR2 effector of the fungal tomato pathogen Cladosporium fulvum, which targets PIP1 and RCR3, and only at apoplastic pH. Importantly, silencing of C14 increased susceptibility to P. infestans, demonstrating that this protease plays a role in pathogen defense. Although C14 is under conservative selection in tomato, it is under diversifying selection in wild potato species (Solanum demissum, Solanum verrucosum, and Solanum stoliniferum) that are the natural hosts of P. infestans. These data reveal a novel effector target in the apoplast that contributes to immunity and is under diversifying selection, but only in the natural host of the pathogen.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kaschani</LastName><ForeName>Farnusch</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Plant Chemetics Laboratory, Chemical Genomics Centre of the Max Planck Society, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shabab</LastName><ForeName>Mohammed</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Bozkurt</LastName><ForeName>Tolga</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Shindo</LastName><ForeName>Takayuki</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Schornack</LastName><ForeName>Sebastian</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Gu</LastName><ForeName>Christian</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Ilyas</LastName><ForeName>Muhammad</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Win</LastName><ForeName>Joe</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Kamoun</LastName><ForeName>Sophien</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>van der Hoorn</LastName><ForeName>Renier A L</ForeName><Initials>RA</Initials></Author></AuthorList><Language>eng</Language><DataBankList 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Physiol</MedlineTA><NlmUniqueID>0401224</NlmUniqueID><ISSNLinking>0032-0889</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018744">DNA, Plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010447">Peptide Hydrolases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018744" MajorTopicYN="N">DNA, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020868" MajorTopicYN="N">Gene Silencing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010447" 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Ilyas</name><name sortKey="Kamoun, Sophien" sort="Kamoun, Sophien" uniqKey="Kamoun S" first="Sophien" last="Kamoun">Sophien Kamoun</name><name sortKey="Schornack, Sebastian" sort="Schornack, Sebastian" uniqKey="Schornack S" first="Sebastian" last="Schornack">Sebastian Schornack</name><name sortKey="Shabab, Mohammed" sort="Shabab, Mohammed" uniqKey="Shabab M" first="Mohammed" last="Shabab">Mohammed Shabab</name><name sortKey="Shindo, Takayuki" sort="Shindo, Takayuki" uniqKey="Shindo T" first="Takayuki" last="Shindo">Takayuki Shindo</name><name sortKey="Van Der Hoorn, Renier A L" sort="Van Der Hoorn, Renier A L" uniqKey="Van Der Hoorn R" first="Renier A L" last="Van Der Hoorn">Renier A L. Van Der Hoorn</name><name sortKey="Win, Joe" sort="Win, Joe" uniqKey="Win J" first="Joe" last="Win">Joe Win</name></noCountry><country name="Allemagne"><region name="Rhénanie-du-Nord-Westphalie"><name sortKey="Kaschani, Farnusch" sort="Kaschani, Farnusch" uniqKey="Kaschani F" first="Farnusch" last="Kaschani">Farnusch Kaschani</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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