Apoplastic effector proteins of plant-associated fungi and oomycetes.
Identifieur interne : 000210 ( Main/Exploration ); précédent : 000209; suivant : 000211Apoplastic effector proteins of plant-associated fungi and oomycetes.
Auteurs : Mercedes Rocafort [Nouvelle-Zélande] ; Isabelle Fudal [France] ; Carl H. Mesarich [Nouvelle-Zélande]Source :
- Current opinion in plant biology [ 1879-0356 ] ; 2020.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Fungal Proteins.
- Fungi, Host-Pathogen Interactions, Oomycetes, Plant Diseases, Plants.
Abstract
The outcome of an interaction between a plant and a fungus or an oomycete, whether compatibility or incompatibility, is often determined in the hostile extracellular spaces and matrices of the apoplast. Indeed, for compatibility to occur, many plant-associated fungi and oomycetes must first neutralize the apoplast, which is both monitored by plant cell-surface immune receptors, and enriched in plant (and frequently, competitor)-derived antimicrobial compounds. Research is highlighting the diverse roles that fungal and oomycete effector proteins play in the apoplast to promote compatibility, with most recent progress made towards understanding the role of these proteins in evading chitin-triggered immunity. Research is also showcasing the ability of apoplastic effector proteins to bring about incompatibility upon recognition by diverse plant cell-surface immune receptors, and the use of effectoromics to rapidly identify apoplastic effector protein-cell-surface immune receptor interactions.
DOI: 10.1016/j.pbi.2020.02.004
PubMed: 32247857
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Indeed, for compatibility to occur, many plant-associated fungi and oomycetes must first neutralize the apoplast, which is both monitored by plant cell-surface immune receptors, and enriched in plant (and frequently, competitor)-derived antimicrobial compounds. Research is highlighting the diverse roles that fungal and oomycete effector proteins play in the apoplast to promote compatibility, with most recent progress made towards understanding the role of these proteins in evading chitin-triggered immunity. Research is also showcasing the ability of apoplastic effector proteins to bring about incompatibility upon recognition by diverse plant cell-surface immune receptors, and the use of effectoromics to rapidly identify apoplastic effector protein-cell-surface immune receptor interactions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Automated" Owner="NLM"><PMID Version="1">32247857</PMID><DateCompleted><Year>2020</Year><Month>10</Month><Day>08</Day></DateCompleted><DateRevised><Year>2020</Year><Month>10</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0356</ISSN><JournalIssue CitedMedium="Internet"><Volume>56</Volume><PubDate><Year>2020</Year><Month>08</Month></PubDate></JournalIssue><Title>Current opinion in plant biology</Title><ISOAbbreviation>Curr Opin Plant Biol</ISOAbbreviation></Journal><ArticleTitle>Apoplastic effector proteins of plant-associated fungi and oomycetes.</ArticleTitle><Pagination><MedlinePgn>9-19</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1369-5266(20)30022-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.pbi.2020.02.004</ELocationID><Abstract><AbstractText>The outcome of an interaction between a plant and a fungus or an oomycete, whether compatibility or incompatibility, is often determined in the hostile extracellular spaces and matrices of the apoplast. Indeed, for compatibility to occur, many plant-associated fungi and oomycetes must first neutralize the apoplast, which is both monitored by plant cell-surface immune receptors, and enriched in plant (and frequently, competitor)-derived antimicrobial compounds. Research is highlighting the diverse roles that fungal and oomycete effector proteins play in the apoplast to promote compatibility, with most recent progress made towards understanding the role of these proteins in evading chitin-triggered immunity. Research is also showcasing the ability of apoplastic effector proteins to bring about incompatibility upon recognition by diverse plant cell-surface immune receptors, and the use of effectoromics to rapidly identify apoplastic effector protein-cell-surface immune receptor interactions.</AbstractText><CopyrightInformation>Copyright © 2020 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rocafort</LastName><ForeName>Mercedes</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory of Molecular Plant Pathology, School of Agriculture and Environment, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fudal</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Université Paris-Saclay, INRAE, AgroParisTech, UMR BIOGER, 78850, Thiverval-Grignon, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mesarich</LastName><ForeName>Carl H</ForeName><Initials>CH</Initials><AffiliationInfo><Affiliation>Laboratory of Molecular Plant Pathology, School of Agriculture and Environment, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand; Bio-Protection Research Centre, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. Electronic address: c.mesarich@massey.ac.nz.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>04</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Curr Opin Plant Biol</MedlineTA><NlmUniqueID>100883395</NlmUniqueID><ISSNLinking>1369-5266</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054884" MajorTopicYN="N">Host-Pathogen Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009868" MajorTopicYN="Y">Oomycetes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="Y">Plant Diseases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>12</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>02</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>02</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>4</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>4</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32247857</ArticleId><ArticleId IdType="pii">S1369-5266(20)30022-4</ArticleId><ArticleId IdType="doi">10.1016/j.pbi.2020.02.004</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li><li>Nouvelle-Zélande</li></country><region><li>Île-de-France</li></region><settlement><li>Thiverval-Grignon</li></settlement></list><tree><country name="Nouvelle-Zélande"><noRegion><name sortKey="Rocafort, Mercedes" sort="Rocafort, Mercedes" uniqKey="Rocafort M" first="Mercedes" last="Rocafort">Mercedes Rocafort</name></noRegion><name sortKey="Mesarich, Carl H" sort="Mesarich, Carl H" uniqKey="Mesarich C" first="Carl H" last="Mesarich">Carl H. Mesarich</name></country><country name="France"><region name="Île-de-France"><name sortKey="Fudal, Isabelle" sort="Fudal, Isabelle" uniqKey="Fudal I" first="Isabelle" last="Fudal">Isabelle Fudal</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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