Signal perception and intracellular signal transduction in plant pathogen defense.
Identifieur interne : 002A31 ( Main/Exploration ); précédent : 002A30; suivant : 002A32Signal perception and intracellular signal transduction in plant pathogen defense.
Auteurs : T. Nürnberger ; W. Wirtz ; D. Nennstiel ; K. Hahlbrock ; T. Jabs ; S. Zimmermann ; D. ScheelSource :
- Journal of receptor and signal transduction research [ 1079-9893 ]
Descripteurs français
- KwdFr :
- Anti-infectieux (métabolisme), Extraits de plantes (biosynthèse), Fabaceae (MeSH), Glycoprotéines membranaires (métabolisme), Immunité innée (MeSH), Magnoliopsida (MeSH), Maladies des plantes (MeSH), Modèles biologiques (MeSH), Mycoses (immunologie), Phytophthora (MeSH), Plantes médicinales (MeSH), Protéines fongiques (métabolisme), Sesquiterpènes (MeSH), Terpènes (MeSH), Transduction du signal (immunologie).
- MESH :
- biosynthèse : Extraits de plantes.
- immunologie : Mycoses, Transduction du signal.
- métabolisme : Anti-infectieux, Glycoprotéines membranaires, Protéines fongiques.
- Fabaceae, Immunité innée, Magnoliopsida, Maladies des plantes, Modèles biologiques, Phytophthora, Plantes médicinales, Sesquiterpènes, Terpènes.
English descriptors
- KwdEn :
- Anti-Infective Agents (metabolism), Fabaceae (MeSH), Fungal Proteins (metabolism), Immunity, Innate (MeSH), Magnoliopsida (MeSH), Membrane Glycoproteins (metabolism), Models, Biological (MeSH), Mycoses (immunology), Phytophthora (MeSH), Plant Diseases (MeSH), Plant Extracts (biosynthesis), Plants, Medicinal (MeSH), Sesquiterpenes (MeSH), Signal Transduction (immunology), Terpenes (MeSH).
- MESH :
- chemical , biosynthesis : Plant Extracts.
- chemical , metabolism : Anti-Infective Agents, Fungal Proteins, Membrane Glycoproteins.
- immunology : Mycoses, Signal Transduction.
- Fabaceae, Immunity, Innate, Magnoliopsida, Models, Biological, Phytophthora, Plant Diseases, Plants, Medicinal, Sesquiterpenes, Terpenes.
Abstract
Disease resistance in plant/pathogen interactions requires sensitive and specific recognition mechanisms for pathogen-derived signals in plants. Cultured parsley (Petroselinum crispum) cells respond to treatment with a crude cell wall preparation derived from the phytopathogenic fungus Phytophthora sojae with transcriptional activation of the same set of defense-related genes as are activated in parsley leaves upon infection with fungal spores. A 13 amino acid core sequence (Pep-13) of a 42 kDa fungal cell wall glycoprotein was identified, which stimulates the same responses as the crude cell wall elicitor, namely macroscopic Ca2+ and H(+)-influxes, effluxes of K(+)- and Cl- ions, production of active oxygen species (oxidative burst), defense-related gene activation, and formation of antifungal phytoalexins. Using [125I]Tyr-Pep-13 as ligand in binding assays, a single-class high-affinity binding site in parsley microsomal membranes and protoplasts could be detected. Binding was specific, saturable, and reversible. By chemical crosslinking, a 91 kDa parsley plasma membrane protein was identified to be the receptor of the peptide elicitor. Isolation of this receptor protein involved in pathogen defense in plants is under way.
DOI: 10.3109/10799899709036598
PubMed: 9029485
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<author><name sortKey="Nurnberger, T" sort="Nurnberger, T" uniqKey="Nurnberger T" first="T" last="Nürnberger">T. Nürnberger</name>
<affiliation><nlm:affiliation>Abt. Stress- und Entwicklungsbiologie, Institut für Pflanzenbiochemie, Halle.</nlm:affiliation>
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<author><name sortKey="Wirtz, W" sort="Wirtz, W" uniqKey="Wirtz W" first="W" last="Wirtz">W. Wirtz</name>
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<author><name sortKey="Nennstiel, D" sort="Nennstiel, D" uniqKey="Nennstiel D" first="D" last="Nennstiel">D. Nennstiel</name>
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<author><name sortKey="Hahlbrock, K" sort="Hahlbrock, K" uniqKey="Hahlbrock K" first="K" last="Hahlbrock">K. Hahlbrock</name>
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<author><name sortKey="Jabs, T" sort="Jabs, T" uniqKey="Jabs T" first="T" last="Jabs">T. Jabs</name>
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<author><name sortKey="Zimmermann, S" sort="Zimmermann, S" uniqKey="Zimmermann S" first="S" last="Zimmermann">S. Zimmermann</name>
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<author><name sortKey="Scheel, D" sort="Scheel, D" uniqKey="Scheel D" first="D" last="Scheel">D. Scheel</name>
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<term>Fabaceae (MeSH)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Immunity, Innate (MeSH)</term>
<term>Magnoliopsida (MeSH)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Models, Biological (MeSH)</term>
<term>Mycoses (immunology)</term>
<term>Phytophthora (MeSH)</term>
<term>Plant Diseases (MeSH)</term>
<term>Plant Extracts (biosynthesis)</term>
<term>Plants, Medicinal (MeSH)</term>
<term>Sesquiterpenes (MeSH)</term>
<term>Signal Transduction (immunology)</term>
<term>Terpenes (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Anti-infectieux (métabolisme)</term>
<term>Extraits de plantes (biosynthèse)</term>
<term>Fabaceae (MeSH)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Immunité innée (MeSH)</term>
<term>Magnoliopsida (MeSH)</term>
<term>Maladies des plantes (MeSH)</term>
<term>Modèles biologiques (MeSH)</term>
<term>Mycoses (immunologie)</term>
<term>Phytophthora (MeSH)</term>
<term>Plantes médicinales (MeSH)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Sesquiterpènes (MeSH)</term>
<term>Terpènes (MeSH)</term>
<term>Transduction du signal (immunologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Plant Extracts</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Anti-Infective Agents</term>
<term>Fungal Proteins</term>
<term>Membrane Glycoproteins</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Extraits de plantes</term>
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<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Mycoses</term>
<term>Transduction du signal</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Mycoses</term>
<term>Signal Transduction</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Anti-infectieux</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines fongiques</term>
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<keywords scheme="MESH" xml:lang="en"><term>Fabaceae</term>
<term>Immunity, Innate</term>
<term>Magnoliopsida</term>
<term>Models, Biological</term>
<term>Phytophthora</term>
<term>Plant Diseases</term>
<term>Plants, Medicinal</term>
<term>Sesquiterpenes</term>
<term>Terpenes</term>
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<term>Immunité innée</term>
<term>Magnoliopsida</term>
<term>Maladies des plantes</term>
<term>Modèles biologiques</term>
<term>Phytophthora</term>
<term>Plantes médicinales</term>
<term>Sesquiterpènes</term>
<term>Terpènes</term>
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<front><div type="abstract" xml:lang="en">Disease resistance in plant/pathogen interactions requires sensitive and specific recognition mechanisms for pathogen-derived signals in plants. Cultured parsley (Petroselinum crispum) cells respond to treatment with a crude cell wall preparation derived from the phytopathogenic fungus Phytophthora sojae with transcriptional activation of the same set of defense-related genes as are activated in parsley leaves upon infection with fungal spores. A 13 amino acid core sequence (Pep-13) of a 42 kDa fungal cell wall glycoprotein was identified, which stimulates the same responses as the crude cell wall elicitor, namely macroscopic Ca2+ and H(+)-influxes, effluxes of K(+)- and Cl- ions, production of active oxygen species (oxidative burst), defense-related gene activation, and formation of antifungal phytoalexins. Using [125I]Tyr-Pep-13 as ligand in binding assays, a single-class high-affinity binding site in parsley microsomal membranes and protoplasts could be detected. Binding was specific, saturable, and reversible. By chemical crosslinking, a 91 kDa parsley plasma membrane protein was identified to be the receptor of the peptide elicitor. Isolation of this receptor protein involved in pathogen defense in plants is under way.</div>
</front>
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<Abstract><AbstractText>Disease resistance in plant/pathogen interactions requires sensitive and specific recognition mechanisms for pathogen-derived signals in plants. Cultured parsley (Petroselinum crispum) cells respond to treatment with a crude cell wall preparation derived from the phytopathogenic fungus Phytophthora sojae with transcriptional activation of the same set of defense-related genes as are activated in parsley leaves upon infection with fungal spores. A 13 amino acid core sequence (Pep-13) of a 42 kDa fungal cell wall glycoprotein was identified, which stimulates the same responses as the crude cell wall elicitor, namely macroscopic Ca2+ and H(+)-influxes, effluxes of K(+)- and Cl- ions, production of active oxygen species (oxidative burst), defense-related gene activation, and formation of antifungal phytoalexins. Using [125I]Tyr-Pep-13 as ligand in binding assays, a single-class high-affinity binding site in parsley microsomal membranes and protoplasts could be detected. Binding was specific, saturable, and reversible. By chemical crosslinking, a 91 kDa parsley plasma membrane protein was identified to be the receptor of the peptide elicitor. Isolation of this receptor protein involved in pathogen defense in plants is under way.</AbstractText>
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<name sortKey="Jabs, T" sort="Jabs, T" uniqKey="Jabs T" first="T" last="Jabs">T. Jabs</name>
<name sortKey="Nennstiel, D" sort="Nennstiel, D" uniqKey="Nennstiel D" first="D" last="Nennstiel">D. Nennstiel</name>
<name sortKey="Nurnberger, T" sort="Nurnberger, T" uniqKey="Nurnberger T" first="T" last="Nürnberger">T. Nürnberger</name>
<name sortKey="Scheel, D" sort="Scheel, D" uniqKey="Scheel D" first="D" last="Scheel">D. Scheel</name>
<name sortKey="Wirtz, W" sort="Wirtz, W" uniqKey="Wirtz W" first="W" last="Wirtz">W. Wirtz</name>
<name sortKey="Zimmermann, S" sort="Zimmermann, S" uniqKey="Zimmermann S" first="S" last="Zimmermann">S. Zimmermann</name>
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