Apoplastic effector proteins of plant-associated fungi and oomycetes.
Identifieur interne : 000171 ( Main/Corpus ); précédent : 000170; suivant : 000172Apoplastic effector proteins of plant-associated fungi and oomycetes.
Auteurs : Mercedes Rocafort ; Isabelle Fudal ; Carl H. MesarichSource :
- Current opinion in plant biology [ 1879-0356 ] ; 2020.
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
Links to Exploration step
pubmed:32247857Le document en format XML
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<author><name sortKey="Fudal, Isabelle" sort="Fudal, Isabelle" uniqKey="Fudal I" first="Isabelle" last="Fudal">Isabelle Fudal</name>
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<author><name sortKey="Mesarich, Carl H" sort="Mesarich, Carl H" uniqKey="Mesarich C" first="Carl H" last="Mesarich">Carl H. Mesarich</name>
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<author><name sortKey="Mesarich, Carl H" sort="Mesarich, Carl H" uniqKey="Mesarich C" first="Carl H" last="Mesarich">Carl H. Mesarich</name>
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<term>Fungi (MeSH)</term>
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<term>Oomycetes (MeSH)</term>
<term>Plant Diseases (MeSH)</term>
<term>Plants (MeSH)</term>
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<front><div type="abstract" xml:lang="en">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.</div>
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<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>
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