A conserved RxLR effector interacts with host RABA-type GTPases to inhibit vesicle-mediated secretion of antimicrobial proteins.
Identifieur interne : 000869 ( Main/Exploration ); précédent : 000868; suivant : 000870A conserved RxLR effector interacts with host RABA-type GTPases to inhibit vesicle-mediated secretion of antimicrobial proteins.
Auteurs : Iga Tomczynska [Suisse] ; Michael Stumpe [Suisse] ; Felix Mauch [Suisse]Source :
- The Plant journal : for cell and molecular biology [ 1365-313X ] ; 2018.
Descripteurs français
- KwdFr :
- Arabidopsis (immunologie), Arabidopsis (microbiologie), Arabidopsis (physiologie), Facteurs de virulence (génétique), Facteurs de virulence (métabolisme), Facteurs de virulence (physiologie), Feuilles de plante (microbiologie), Immunoprécipitation (MeSH), Interactions hôte-pathogène (MeSH), Maladies des plantes (immunologie), Maladies des plantes (microbiologie), Peptides antimicrobiens cationiques (métabolisme), Phytophthora (génétique), Phytophthora (métabolisme), Phytophthora (physiologie), Protéines G rab (métabolisme), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Protéines fongiques (physiologie), Solanum tuberosum (immunologie), Solanum tuberosum (microbiologie), Solanum tuberosum (physiologie), Vésicules extracellulaires (métabolisme).
- MESH :
- génétique : Facteurs de virulence, Phytophthora, Protéines fongiques.
- immunologie : Arabidopsis, Maladies des plantes, Solanum tuberosum.
- microbiologie : Arabidopsis, Feuilles de plante, Maladies des plantes, Solanum tuberosum.
- métabolisme : Facteurs de virulence, Peptides antimicrobiens cationiques, Phytophthora, Protéines G rab, Protéines fongiques, Vésicules extracellulaires.
- physiologie : Arabidopsis, Facteurs de virulence, Phytophthora, Protéines fongiques, Solanum tuberosum.
- Immunoprécipitation, Interactions hôte-pathogène.
English descriptors
- KwdEn :
- Antimicrobial Cationic Peptides (metabolism), Arabidopsis (immunology), Arabidopsis (microbiology), Arabidopsis (physiology), Extracellular Vesicles (metabolism), Fungal Proteins (genetics), Fungal Proteins (metabolism), Fungal Proteins (physiology), Host-Pathogen Interactions (MeSH), Immunoprecipitation (MeSH), Phytophthora (genetics), Phytophthora (metabolism), Phytophthora (physiology), Plant Diseases (immunology), Plant Diseases (microbiology), Plant Leaves (microbiology), Solanum tuberosum (immunology), Solanum tuberosum (microbiology), Solanum tuberosum (physiology), Virulence Factors (genetics), Virulence Factors (metabolism), Virulence Factors (physiology), rab GTP-Binding Proteins (metabolism).
- MESH :
- chemical , genetics : Fungal Proteins, Virulence Factors.
- chemical , metabolism : Antimicrobial Cationic Peptides, Fungal Proteins, Virulence Factors, rab GTP-Binding Proteins.
- genetics : Phytophthora.
- immunology : Arabidopsis, Plant Diseases, Solanum tuberosum.
- metabolism : Extracellular Vesicles, Phytophthora.
- microbiology : Arabidopsis, Plant Diseases, Plant Leaves, Solanum tuberosum.
- physiology : Arabidopsis, Fungal Proteins, Phytophthora, Solanum tuberosum, Virulence Factors.
- Host-Pathogen Interactions, Immunoprecipitation.
Abstract
Plant pathogens of the oomycete genus Phytophthora produce virulence factors, known as RxLR effector proteins that are transferred into host cells to suppress disease resistance. Here, we analyse the function of the highly conserved RxLR24 effector of Phytophthora brassicae. RxLR24 was expressed early in the interaction with Arabidopsis plants and ectopic expression in the host enhanced leaf colonization and zoosporangia formation. Co-immunoprecipitation (Co-IP) experiments followed by mass spectrometry identified different members of the RABA GTPase family as putative RxLR24 targets. Physical interaction of RxLR24 or its homologue from the potato pathogen Phytophthora infestans with different RABA GTPases of Arabidopsis or potato, respectively, was confirmed by reciprocal Co-IP. In line with the function of RABA GTPases in vesicular secretion, RxLR24 co-localized with RABA1a to vesicles and the plasma membrane. The effect of RxLR24 on the secretory process was analysed with fusion constructs of secreted antimicrobial proteins with a pH-sensitive GFP tag. PATHOGENESIS RELATED PROTEIN 1 (PR-1) and DEFENSIN (PDF1.2) were efficiently exported in control tissue, whereas in the presence of RxLR24 they both accumulated in the endoplasmic reticulum. Together our results imply a virulence function of RxLR24 effectors as inhibitors of RABA GTPase-mediated vesicular secretion of antimicrobial PR-1, PDF1.2 and possibly other defence-related compounds.
DOI: 10.1111/tpj.13928
PubMed: 29671919
Affiliations:
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Here, we analyse the function of the highly conserved RxLR24 effector of Phytophthora brassicae. RxLR24 was expressed early in the interaction with Arabidopsis plants and ectopic expression in the host enhanced leaf colonization and zoosporangia formation. Co-immunoprecipitation (Co-IP) experiments followed by mass spectrometry identified different members of the RABA GTPase family as putative RxLR24 targets. Physical interaction of RxLR24 or its homologue from the potato pathogen Phytophthora infestans with different RABA GTPases of Arabidopsis or potato, respectively, was confirmed by reciprocal Co-IP. In line with the function of RABA GTPases in vesicular secretion, RxLR24 co-localized with RABA1a to vesicles and the plasma membrane. The effect of RxLR24 on the secretory process was analysed with fusion constructs of secreted antimicrobial proteins with a pH-sensitive GFP tag. PATHOGENESIS RELATED PROTEIN 1 (PR-1) and DEFENSIN (PDF1.2) were efficiently exported in control tissue, whereas in the presence of RxLR24 they both accumulated in the endoplasmic reticulum. Together our results imply a virulence function of RxLR24 effectors as inhibitors of RABA GTPase-mediated vesicular secretion of antimicrobial PR-1, PDF1.2 and possibly other defence-related compounds.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29671919</PMID><DateCompleted><Year>2019</Year><Month>06</Month><Day>03</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>03</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1365-313X</ISSN><JournalIssue CitedMedium="Internet"><Volume>95</Volume><Issue>2</Issue><PubDate><Year>2018</Year><Month>07</Month></PubDate></JournalIssue><Title>The Plant journal : for cell and molecular biology</Title><ISOAbbreviation>Plant J</ISOAbbreviation></Journal><ArticleTitle>A conserved RxLR effector interacts with host RABA-type GTPases to inhibit vesicle-mediated secretion of antimicrobial proteins.</ArticleTitle><Pagination><MedlinePgn>187-203</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/tpj.13928</ELocationID><Abstract><AbstractText>Plant pathogens of the oomycete genus Phytophthora produce virulence factors, known as RxLR effector proteins that are transferred into host cells to suppress disease resistance. Here, we analyse the function of the highly conserved RxLR24 effector of Phytophthora brassicae. RxLR24 was expressed early in the interaction with Arabidopsis plants and ectopic expression in the host enhanced leaf colonization and zoosporangia formation. Co-immunoprecipitation (Co-IP) experiments followed by mass spectrometry identified different members of the RABA GTPase family as putative RxLR24 targets. Physical interaction of RxLR24 or its homologue from the potato pathogen Phytophthora infestans with different RABA GTPases of Arabidopsis or potato, respectively, was confirmed by reciprocal Co-IP. In line with the function of RABA GTPases in vesicular secretion, RxLR24 co-localized with RABA1a to vesicles and the plasma membrane. The effect of RxLR24 on the secretory process was analysed with fusion constructs of secreted antimicrobial proteins with a pH-sensitive GFP tag. PATHOGENESIS RELATED PROTEIN 1 (PR-1) and DEFENSIN (PDF1.2) were efficiently exported in control tissue, whereas in the presence of RxLR24 they both accumulated in the endoplasmic reticulum. Together our results imply a virulence function of RxLR24 effectors as inhibitors of RABA GTPase-mediated vesicular secretion of antimicrobial PR-1, PDF1.2 and possibly other defence-related compounds.</AbstractText><CopyrightInformation>© 2018 The Authors The Plant Journal © 2018 John Wiley & Sons Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tomczynska</LastName><ForeName>Iga</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Fribourg, chemin du musée 10, 1700, Fribourg, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Stumpe</LastName><ForeName>Michael</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Fribourg, chemin du musée 10, 1700, Fribourg, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mauch</LastName><ForeName>Felix</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Fribourg, chemin du musée 10, 1700, Fribourg, Switzerland.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList 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DateType="Electronic"><Year>2018</Year><Month>05</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Plant J</MedlineTA><NlmUniqueID>9207397</NlmUniqueID><ISSNLinking>0960-7412</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D023181">Antimicrobial Cationic Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037521">Virulence Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.5.2</RegistryNumber><NameOfSubstance UI="D020691">rab GTP-Binding Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Plant J. 2018 Jul;95(2):185-186</RefSource><PMID Version="1">29971852</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D023181" MajorTopicYN="N">Antimicrobial Cationic Peptides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000067128" MajorTopicYN="N">Extracellular Vesicles</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054884" MajorTopicYN="N">Host-Pathogen Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047468" MajorTopicYN="N">Immunoprecipitation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018515" MajorTopicYN="N">Plant Leaves</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011198" MajorTopicYN="N">Solanum tuberosum</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D037521" MajorTopicYN="N">Virulence Factors</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020691" MajorTopicYN="N">rab GTP-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Arabidopsis thaliana
</Keyword><Keyword MajorTopicYN="Y">Solanum tuberosum
</Keyword><Keyword MajorTopicYN="Y">Phytophthora</Keyword><Keyword MajorTopicYN="Y">RABA GTPases</Keyword><Keyword MajorTopicYN="Y">RxLR effector</Keyword><Keyword MajorTopicYN="Y">plant immunity</Keyword><Keyword MajorTopicYN="Y">secretion</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>11</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>03</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>03</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>4</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>6</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>4</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29671919</ArticleId><ArticleId IdType="doi">10.1111/tpj.13928</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country><region><li>Canton de Fribourg</li></region><settlement><li>Fribourg</li></settlement><orgName><li>Université de Fribourg</li></orgName></list><tree><country name="Suisse"><region name="Canton de Fribourg"><name sortKey="Tomczynska, Iga" sort="Tomczynska, Iga" uniqKey="Tomczynska I" first="Iga" last="Tomczynska">Iga Tomczynska</name></region><name sortKey="Mauch, Felix" sort="Mauch, Felix" uniqKey="Mauch F" first="Felix" last="Mauch">Felix Mauch</name><name sortKey="Stumpe, Michael" sort="Stumpe, Michael" uniqKey="Stumpe M" first="Michael" last="Stumpe">Michael Stumpe</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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