Phosphoproteomic analysis of induced resistance reveals activation of signal transduction processes by beneficial and pathogenic interaction in grapevine.
Identifieur interne : 000372 ( Main/Exploration ); précédent : 000371; suivant : 000373Phosphoproteomic analysis of induced resistance reveals activation of signal transduction processes by beneficial and pathogenic interaction in grapevine.
Auteurs : Michele Perazzolli [Italie] ; Maria Cristina Palmieri [Italie] ; Vittoria Matafora [Italie] ; Angela Bachi [Italie] ; Ilaria Pertot [Italie]Source :
- Journal of plant physiology [ 1618-1328 ] ; 2016.
Descripteurs français
- KwdFr :
- Feuilles de plante (immunologie), Feuilles de plante (microbiologie), Feuilles de plante (physiologie), Interactions hôte-pathogène (MeSH), Maladies des plantes (immunologie), Maladies des plantes (microbiologie), Maturation post-traductionnelle des protéines (MeSH), Mitogen-Activated Protein Kinases (métabolisme), Oomycetes (physiologie), Phosphorylation (MeSH), Protéines végétales (métabolisme), Protéomique (MeSH), Résistance à la maladie (MeSH), Transduction du signal (MeSH), Trichoderma (physiologie), Vitis (immunologie), Vitis (microbiologie), Vitis (physiologie).
- MESH :
- immunologie : Feuilles de plante, Maladies des plantes, Vitis.
- microbiologie : Feuilles de plante, Maladies des plantes, Vitis.
- métabolisme : Mitogen-Activated Protein Kinases, Protéines végétales.
- physiologie : Feuilles de plante, Oomycetes, Trichoderma, Vitis.
- Interactions hôte-pathogène, Maturation post-traductionnelle des protéines, Phosphorylation, Protéomique, Résistance à la maladie, Transduction du signal.
English descriptors
- KwdEn :
- Disease Resistance (MeSH), Host-Pathogen Interactions (MeSH), Mitogen-Activated Protein Kinases (metabolism), Oomycetes (physiology), Phosphorylation (MeSH), Plant Diseases (immunology), Plant Diseases (microbiology), Plant Leaves (immunology), Plant Leaves (microbiology), Plant Leaves (physiology), Plant Proteins (metabolism), Protein Processing, Post-Translational (MeSH), Proteomics (MeSH), Signal Transduction (MeSH), Trichoderma (physiology), Vitis (immunology), Vitis (microbiology), Vitis (physiology).
- MESH :
- chemical , metabolism : Mitogen-Activated Protein Kinases, Plant Proteins.
- immunology : Plant Diseases, Plant Leaves, Vitis.
- microbiology : Plant Diseases, Plant Leaves, Vitis.
- physiology : Oomycetes, Plant Leaves, Trichoderma, Vitis.
- Disease Resistance, Host-Pathogen Interactions, Phosphorylation, Protein Processing, Post-Translational, Proteomics, Signal Transduction.
Abstract
Protein phosphorylation regulates several key processes of the plant immune system. Protein kinases and phosphatases are pivotal regulators of defense mechanisms elicited by resistance inducers. However, the phosphorylation cascades that trigger the induced resistance mechanisms in plants have not yet been deeply investigated. The beneficial fungus Trichoderma harzianum T39 (T39) induces resistance against grapevine downy mildew (Plasmopara viticola), but its efficacy could be further improved by a better understanding of the cellular regulations involved. We investigated quantitative changes in the grapevine phosphoproteome during T39-induced resistance to get an overview of regulatory mechanisms of downy mildew resistance. Immunodetection experiments revealed activation of the 45 and 49kDa kinases by T39 treatment both before and after pathogen inoculation, and the phosphoproteomic analysis identified 103 phosphopeptides that were significantly affected by the phosphorylation cascades during T39-induced resistance. Peptides affected by T39 treatment showed comparable phosphorylation levels after P. viticola inoculation, indicating activation of the microbial recognition machinery before pathogen infection. Phosphorylation profiles of proteins related to photosynthetic processes and protein ubiquitination indicated a partial overlap of cellular responses in T39-treated and control plants. However, phosphorylation changes of proteins involved in response to stimuli, signal transduction, hormone signaling, gene expression regulation, and RNA metabolism were exclusively elicited by P. viticola inoculation in T39-treated plants. These results highlighted the relevance of phosphorylation changes during T39-induced resistance and identified key regulator candidates of the grapevine defense against downy mildew.
DOI: 10.1016/j.jplph.2016.03.007
PubMed: 27010348
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Mach 1, 38010 San Michele all'Adige, Italy. Electronic address: michele.perazzolli@fmach.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Sustainable Agro-ecosystems and Bioresources, Research and Innovation Centre, Fondazione Edmund Mach (FEM), Via E. Mach 1, 38010 San Michele all'Adige</wicri:regionArea><wicri:noRegion>38010 San Michele all'Adige</wicri:noRegion></affiliation></author><author><name sortKey="Palmieri, Maria Cristina" sort="Palmieri, Maria Cristina" uniqKey="Palmieri M" first="Maria Cristina" last="Palmieri">Maria Cristina Palmieri</name><affiliation wicri:level="1"><nlm:affiliation>Department of Sustainable Agro-ecosystems and Bioresources, Research and Innovation Centre, Fondazione Edmund Mach (FEM), Via E. Mach 1, 38010 San Michele all'Adige, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Sustainable Agro-ecosystems and Bioresources, Research and Innovation Centre, Fondazione Edmund Mach (FEM), Via E. 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Mach 1, 38010 San Michele all'Adige, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Sustainable Agro-ecosystems and Bioresources, Research and Innovation Centre, Fondazione Edmund Mach (FEM), Via E. Mach 1, 38010 San Michele all'Adige</wicri:regionArea><wicri:noRegion>38010 San Michele all'Adige</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of plant physiology</title><idno type="eISSN">1618-1328</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Disease Resistance (MeSH)</term><term>Host-Pathogen Interactions (MeSH)</term><term>Mitogen-Activated Protein Kinases (metabolism)</term><term>Oomycetes (physiology)</term><term>Phosphorylation (MeSH)</term><term>Plant Diseases (immunology)</term><term>Plant Diseases (microbiology)</term><term>Plant Leaves (immunology)</term><term>Plant Leaves (microbiology)</term><term>Plant Leaves (physiology)</term><term>Plant Proteins (metabolism)</term><term>Protein Processing, Post-Translational (MeSH)</term><term>Proteomics (MeSH)</term><term>Signal Transduction (MeSH)</term><term>Trichoderma (physiology)</term><term>Vitis (immunology)</term><term>Vitis (microbiology)</term><term>Vitis (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Feuilles de plante (immunologie)</term><term>Feuilles de plante (microbiologie)</term><term>Feuilles de plante (physiologie)</term><term>Interactions hôte-pathogène (MeSH)</term><term>Maladies des plantes (immunologie)</term><term>Maladies des plantes (microbiologie)</term><term>Maturation post-traductionnelle des protéines (MeSH)</term><term>Mitogen-Activated Protein Kinases (métabolisme)</term><term>Oomycetes (physiologie)</term><term>Phosphorylation (MeSH)</term><term>Protéines végétales (métabolisme)</term><term>Protéomique (MeSH)</term><term>Résistance à la maladie (MeSH)</term><term>Transduction du signal (MeSH)</term><term>Trichoderma (physiologie)</term><term>Vitis (immunologie)</term><term>Vitis (microbiologie)</term><term>Vitis (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Mitogen-Activated Protein Kinases</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Feuilles de plante</term><term>Maladies des plantes</term><term>Vitis</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Plant Diseases</term><term>Plant Leaves</term><term>Vitis</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Feuilles de plante</term><term>Maladies des plantes</term><term>Vitis</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Plant Diseases</term><term>Plant Leaves</term><term>Vitis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Mitogen-Activated Protein Kinases</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Feuilles de plante</term><term>Oomycetes</term><term>Trichoderma</term><term>Vitis</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Oomycetes</term><term>Plant Leaves</term><term>Trichoderma</term><term>Vitis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Disease Resistance</term><term>Host-Pathogen Interactions</term><term>Phosphorylation</term><term>Protein Processing, Post-Translational</term><term>Proteomics</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Interactions hôte-pathogène</term><term>Maturation post-traductionnelle des protéines</term><term>Phosphorylation</term><term>Protéomique</term><term>Résistance à la maladie</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Protein phosphorylation regulates several key processes of the plant immune system. Protein kinases and phosphatases are pivotal regulators of defense mechanisms elicited by resistance inducers. However, the phosphorylation cascades that trigger the induced resistance mechanisms in plants have not yet been deeply investigated. The beneficial fungus Trichoderma harzianum T39 (T39) induces resistance against grapevine downy mildew (Plasmopara viticola), but its efficacy could be further improved by a better understanding of the cellular regulations involved. We investigated quantitative changes in the grapevine phosphoproteome during T39-induced resistance to get an overview of regulatory mechanisms of downy mildew resistance. Immunodetection experiments revealed activation of the 45 and 49kDa kinases by T39 treatment both before and after pathogen inoculation, and the phosphoproteomic analysis identified 103 phosphopeptides that were significantly affected by the phosphorylation cascades during T39-induced resistance. Peptides affected by T39 treatment showed comparable phosphorylation levels after P. viticola inoculation, indicating activation of the microbial recognition machinery before pathogen infection. Phosphorylation profiles of proteins related to photosynthetic processes and protein ubiquitination indicated a partial overlap of cellular responses in T39-treated and control plants. However, phosphorylation changes of proteins involved in response to stimuli, signal transduction, hormone signaling, gene expression regulation, and RNA metabolism were exclusively elicited by P. viticola inoculation in T39-treated plants. These results highlighted the relevance of phosphorylation changes during T39-induced resistance and identified key regulator candidates of the grapevine defense against downy mildew. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27010348</PMID><DateCompleted><Year>2017</Year><Month>02</Month><Day>13</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1618-1328</ISSN><JournalIssue CitedMedium="Internet"><Volume>195</Volume><PubDate><Year>2016</Year><Month>May</Month><Day>20</Day></PubDate></JournalIssue><Title>Journal of plant physiology</Title><ISOAbbreviation>J Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Phosphoproteomic analysis of induced resistance reveals activation of signal transduction processes by beneficial and pathogenic interaction in grapevine.</ArticleTitle><Pagination><MedlinePgn>59-72</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jplph.2016.03.007</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0176-1617(16)00066-3</ELocationID><Abstract><AbstractText>Protein phosphorylation regulates several key processes of the plant immune system. Protein kinases and phosphatases are pivotal regulators of defense mechanisms elicited by resistance inducers. However, the phosphorylation cascades that trigger the induced resistance mechanisms in plants have not yet been deeply investigated. The beneficial fungus Trichoderma harzianum T39 (T39) induces resistance against grapevine downy mildew (Plasmopara viticola), but its efficacy could be further improved by a better understanding of the cellular regulations involved. We investigated quantitative changes in the grapevine phosphoproteome during T39-induced resistance to get an overview of regulatory mechanisms of downy mildew resistance. Immunodetection experiments revealed activation of the 45 and 49kDa kinases by T39 treatment both before and after pathogen inoculation, and the phosphoproteomic analysis identified 103 phosphopeptides that were significantly affected by the phosphorylation cascades during T39-induced resistance. Peptides affected by T39 treatment showed comparable phosphorylation levels after P. viticola inoculation, indicating activation of the microbial recognition machinery before pathogen infection. Phosphorylation profiles of proteins related to photosynthetic processes and protein ubiquitination indicated a partial overlap of cellular responses in T39-treated and control plants. However, phosphorylation changes of proteins involved in response to stimuli, signal transduction, hormone signaling, gene expression regulation, and RNA metabolism were exclusively elicited by P. viticola inoculation in T39-treated plants. These results highlighted the relevance of phosphorylation changes during T39-induced resistance and identified key regulator candidates of the grapevine defense against downy mildew. </AbstractText><CopyrightInformation>Copyright © 2016 Elsevier GmbH. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Perazzolli</LastName><ForeName>Michele</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Sustainable Agro-ecosystems and Bioresources, Research and Innovation Centre, Fondazione Edmund Mach (FEM), Via E. Mach 1, 38010 San Michele all'Adige, Italy. Electronic address: michele.perazzolli@fmach.it.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Palmieri</LastName><ForeName>Maria Cristina</ForeName><Initials>MC</Initials><AffiliationInfo><Affiliation>Department of Sustainable Agro-ecosystems and Bioresources, Research and Innovation Centre, Fondazione Edmund Mach (FEM), Via E. Mach 1, 38010 San Michele all'Adige, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matafora</LastName><ForeName>Vittoria</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Biological Mass Spectrometry Unit DIBIT, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milano, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bachi</LastName><ForeName>Angela</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Biological Mass Spectrometry Unit DIBIT, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milano, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pertot</LastName><ForeName>Ilaria</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Department of Sustainable Agro-ecosystems and Bioresources, Research and Innovation Centre, Fondazione Edmund Mach (FEM), Via E. Mach 1, 38010 San Michele all'Adige, Italy.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>03</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>J Plant Physiol</MedlineTA><NlmUniqueID>9882059</NlmUniqueID><ISSNLinking>0176-1617</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.24</RegistryNumber><NameOfSubstance UI="D020928">Mitogen-Activated Protein Kinases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D060467" MajorTopicYN="N">Disease Resistance</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054884" MajorTopicYN="Y">Host-Pathogen Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020928" MajorTopicYN="N">Mitogen-Activated Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009868" MajorTopicYN="N">Oomycetes</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018515" MajorTopicYN="N">Plant Leaves</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D040901" MajorTopicYN="N">Proteomics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014242" MajorTopicYN="N">Trichoderma</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D027843" MajorTopicYN="N">Vitis</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Gel-free proteomics</Keyword><Keyword MajorTopicYN="N">Induced resistance</Keyword><Keyword MajorTopicYN="N">Phosphoproteomics</Keyword><Keyword MajorTopicYN="N">Plant defense</Keyword><Keyword MajorTopicYN="N">Post-translational modifications</Keyword><Keyword MajorTopicYN="N">Vitis vinifera</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>02</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>03</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>03</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>3</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>3</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>2</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27010348</ArticleId><ArticleId IdType="pii">S0176-1617(16)00066-3</ArticleId><ArticleId IdType="doi">10.1016/j.jplph.2016.03.007</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><country name="Italie"><noRegion><name sortKey="Perazzolli, Michele" sort="Perazzolli, Michele" uniqKey="Perazzolli M" first="Michele" last="Perazzolli">Michele Perazzolli</name></noRegion><name sortKey="Bachi, Angela" sort="Bachi, Angela" uniqKey="Bachi A" first="Angela" last="Bachi">Angela Bachi</name><name sortKey="Matafora, Vittoria" sort="Matafora, Vittoria" uniqKey="Matafora V" first="Vittoria" last="Matafora">Vittoria Matafora</name><name sortKey="Palmieri, Maria Cristina" sort="Palmieri, Maria Cristina" uniqKey="Palmieri M" first="Maria Cristina" last="Palmieri">Maria Cristina Palmieri</name><name sortKey="Pertot, Ilaria" sort="Pertot, Ilaria" uniqKey="Pertot I" first="Ilaria" last="Pertot">Ilaria Pertot</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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