Serveur d'exploration Phytophthora

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High-affinity binding of a synthetic heptaglucoside and fungal glucan phytoalexin elicitors to soybean membranes.

Identifieur interne : 002D27 ( Main/Exploration ); précédent : 002D26; suivant : 002D28

High-affinity binding of a synthetic heptaglucoside and fungal glucan phytoalexin elicitors to soybean membranes.

Auteurs : E G Cosio [Allemagne] ; T. Frey ; R. Verduyn ; J. Van Boom ; J. Ebel

Source :

RBID : pubmed:2226806

Descripteurs français

English descriptors

Abstract

Soybean membranes possess high-affinity binding sites for fungal beta-glucans that elicit phytoalexin synthesis. The ability of 1,3-1,6-beta-glucans, released by acid hydrolysis from mycelial walls of Phytophthora megasperma f.sp. glycinea, to compete for the putative phytoalexin elicitor receptors increases with their average degree of polymerization (DP). The results suggest a function where the probability for glucan fragments of containing a structural determinant that is optimal for binding approaches 1 as the DP tends to infinity. Ligand displacement data obtained against a 125I-labeled glucan elicitor (average DP = 18) provided a theoretical minimum IC50 (50% inhibitory concentration) for 1,3-1,6-beta-glucans of 3 nM. The IC50 value obtained for a synthetic hepta-beta-glucoside having a known elicitor-active structure was 8 nM, remarkably close to the predicted value. Displacement of the 125I-glucan of large DP was uniform and complete showing that the heptaglucoside had access, with similar affinity, to all sites available to the radioligand. Further analysis using a 125I-labeled aminophenethylamine derivative of the heptaglucoside suggested that the putative glucan-elicitor receptors bind a basic structural determinant present in all elicitor-active glucans from the soybean pathogen P. megasperma.

DOI: 10.1016/0014-5793(90)80411-b
PubMed: 2226806


Affiliations:


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Le document en format XML

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<title xml:lang="en">High-affinity binding of a synthetic heptaglucoside and fungal glucan phytoalexin elicitors to soybean membranes.</title>
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<name sortKey="Cosio, E G" sort="Cosio, E G" uniqKey="Cosio E" first="E G" last="Cosio">E G Cosio</name>
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<nlm:affiliation>Lehrstuhl für Biochemie der Pflanzen, Biologisches Institut II der Universität, Freiburg, FRG.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
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<name sortKey="Frey, T" sort="Frey, T" uniqKey="Frey T" first="T" last="Frey">T. Frey</name>
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<name sortKey="Verduyn, R" sort="Verduyn, R" uniqKey="Verduyn R" first="R" last="Verduyn">R. Verduyn</name>
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<name sortKey="Van Boom, J" sort="Van Boom, J" uniqKey="Van Boom J" first="J" last="Van Boom">J. Van Boom</name>
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<term>Binding, Competitive (MeSH)</term>
<term>Cell Membrane (metabolism)</term>
<term>Glucans (metabolism)</term>
<term>Glucosides (metabolism)</term>
<term>Phytophthora (analysis)</term>
<term>Plant Extracts (metabolism)</term>
<term>Sesquiterpenes (MeSH)</term>
<term>Soybeans (metabolism)</term>
<term>Terpenes (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Extraits de plantes (métabolisme)</term>
<term>Fixation compétitive (MeSH)</term>
<term>Glucanes (métabolisme)</term>
<term>Glucosides (métabolisme)</term>
<term>Membrane cellulaire (métabolisme)</term>
<term>Phytophthora (analyse)</term>
<term>Sesquiterpènes (MeSH)</term>
<term>Soja (métabolisme)</term>
<term>Terpènes (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Glucans</term>
<term>Glucosides</term>
<term>Plant Extracts</term>
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<keywords scheme="MESH" qualifier="analyse" xml:lang="fr">
<term>Phytophthora</term>
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<term>Phytophthora</term>
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<term>Cell Membrane</term>
<term>Soybeans</term>
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<term>Extraits de plantes</term>
<term>Glucanes</term>
<term>Glucosides</term>
<term>Membrane cellulaire</term>
<term>Soja</term>
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<term>Sesquiterpenes</term>
<term>Terpenes</term>
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<front>
<div type="abstract" xml:lang="en">Soybean membranes possess high-affinity binding sites for fungal beta-glucans that elicit phytoalexin synthesis. The ability of 1,3-1,6-beta-glucans, released by acid hydrolysis from mycelial walls of Phytophthora megasperma f.sp. glycinea, to compete for the putative phytoalexin elicitor receptors increases with their average degree of polymerization (DP). The results suggest a function where the probability for glucan fragments of containing a structural determinant that is optimal for binding approaches 1 as the DP tends to infinity. Ligand displacement data obtained against a 125I-labeled glucan elicitor (average DP = 18) provided a theoretical minimum IC50 (50% inhibitory concentration) for 1,3-1,6-beta-glucans of 3 nM. The IC50 value obtained for a synthetic hepta-beta-glucoside having a known elicitor-active structure was 8 nM, remarkably close to the predicted value. Displacement of the 125I-glucan of large DP was uniform and complete showing that the heptaglucoside had access, with similar affinity, to all sites available to the radioligand. Further analysis using a 125I-labeled aminophenethylamine derivative of the heptaglucoside suggested that the putative glucan-elicitor receptors bind a basic structural determinant present in all elicitor-active glucans from the soybean pathogen P. megasperma.</div>
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<Issue>1-2</Issue>
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<AbstractText>Soybean membranes possess high-affinity binding sites for fungal beta-glucans that elicit phytoalexin synthesis. The ability of 1,3-1,6-beta-glucans, released by acid hydrolysis from mycelial walls of Phytophthora megasperma f.sp. glycinea, to compete for the putative phytoalexin elicitor receptors increases with their average degree of polymerization (DP). The results suggest a function where the probability for glucan fragments of containing a structural determinant that is optimal for binding approaches 1 as the DP tends to infinity. Ligand displacement data obtained against a 125I-labeled glucan elicitor (average DP = 18) provided a theoretical minimum IC50 (50% inhibitory concentration) for 1,3-1,6-beta-glucans of 3 nM. The IC50 value obtained for a synthetic hepta-beta-glucoside having a known elicitor-active structure was 8 nM, remarkably close to the predicted value. Displacement of the 125I-glucan of large DP was uniform and complete showing that the heptaglucoside had access, with similar affinity, to all sites available to the radioligand. Further analysis using a 125I-labeled aminophenethylamine derivative of the heptaglucoside suggested that the putative glucan-elicitor receptors bind a basic structural determinant present in all elicitor-active glucans from the soybean pathogen P. megasperma.</AbstractText>
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<LastName>Cosio</LastName>
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<Affiliation>Lehrstuhl für Biochemie der Pflanzen, Biologisches Institut II der Universität, Freiburg, FRG.</Affiliation>
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<name sortKey="Cosio, E G" sort="Cosio, E G" uniqKey="Cosio E" first="E G" last="Cosio">E G Cosio</name>
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