Serveur d'exploration Phytophthora

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Physiological and proteomic approaches to evaluate the role of sterol binding in elicitin-induced resistance.

Identifieur interne : 001471 ( Main/Exploration ); précédent : 001470; suivant : 001472

Physiological and proteomic approaches to evaluate the role of sterol binding in elicitin-induced resistance.

Auteurs : Ladislav Dokládal [République tchèque] ; Michal Oboril ; Karel Stejskal ; Zbynek Zdráhal ; Nikola Ptácková ; Radka Chaloupková ; Jirí Damborsky ; Tomás Kasparovsky ; Sylvain Jeandroz ; Markéta Zd'Árská ; Jan Lochman

Source :

RBID : pubmed:22223811

Descripteurs français

English descriptors

Abstract

Cryptogein is a proteinaceous elicitor secreted by Phytophthora cryptogea that can induce resistance to P. parasitica in tobacco plants. On the basis of previous computer modelling experiments, by site-directed mutagenesis a series of cryptogein variants was prepared with altered abilities to bind sterols, phospholipids or both. The sterol binding and phospholipid transfer activities corresponded well with the previously reported structural data. Induction of the synthesis of reactive oxygen species (ROS) in tobacco cells in suspension and proteomic analysis of intercellular fluid changes in tobacco leaves triggered by these mutant proteins were not proportional to their ability to bind or transfer sterols and phospholipids. However, changes in the intercellular proteome corresponded to transcription levels of defence genes and resistance to P. parasitica and structure-prediction of mutants did not reveal any significant changes in protein structure. These results suggest, contrary to previous proposals, that the sterol-binding ability of cryptogein and its mutants, and the associated conformational change in the ω-loop, might not be principal factors in either ROS production or resistance induction. Nevertheless, the results support the importance of the ω-loop for the interaction of the protein with the high affinity binding site on the plasma membrane.

DOI: 10.1093/jxb/err427
PubMed: 22223811
PubMed Central: PMC3295402


Affiliations:


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Le document en format XML

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<term>Mutation (MeSH)</term>
<term>Phospholipids (metabolism)</term>
<term>Phytophthora (genetics)</term>
<term>Phytophthora (metabolism)</term>
<term>Phytophthora (pathogenicity)</term>
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<term>Plant Diseases (parasitology)</term>
<term>Plant Immunity (immunology)</term>
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<term>Plant Leaves (immunology)</term>
<term>Plant Leaves (parasitology)</term>
<term>Plant Leaves (physiology)</term>
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<term>Proteins (metabolism)</term>
<term>Proteomics (methods)</term>
<term>Reactive Oxygen Species (metabolism)</term>
<term>Recombinant Proteins (MeSH)</term>
<term>Sesquiterpenes (analysis)</term>
<term>Sterols (metabolism)</term>
<term>Structure-Activity Relationship (MeSH)</term>
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<term>Tobacco (immunology)</term>
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<term>Feuilles de plante (génétique)</term>
<term>Feuilles de plante (immunologie)</term>
<term>Feuilles de plante (parasitologie)</term>
<term>Feuilles de plante (physiologie)</term>
<term>Immunité des plantes (immunologie)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Maladies des plantes (immunologie)</term>
<term>Maladies des plantes (parasitologie)</term>
<term>Mutation (MeSH)</term>
<term>Phospholipides (métabolisme)</term>
<term>Phytophthora (génétique)</term>
<term>Phytophthora (métabolisme)</term>
<term>Phytophthora (pathogénicité)</term>
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<term>Protéines fongiques (métabolisme)</term>
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<term>Protéomique (méthodes)</term>
<term>Relation structure-activité (MeSH)</term>
<term>Sesquiterpènes (analyse)</term>
<term>Stérols (métabolisme)</term>
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<term>Tabac (immunologie)</term>
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<term>Phytophthora</term>
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<term>Proteomics</term>
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<term>Espèces réactives de l'oxygène</term>
<term>Phospholipides</term>
<term>Phytophthora</term>
<term>Protéines</term>
<term>Protéines fongiques</term>
<term>Stérols</term>
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<term>Protéomique</term>
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<term>Maladies des plantes</term>
<term>Tabac</term>
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<term>Mutation</term>
<term>Protéines recombinantes</term>
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<div type="abstract" xml:lang="en">Cryptogein is a proteinaceous elicitor secreted by Phytophthora cryptogea that can induce resistance to P. parasitica in tobacco plants. On the basis of previous computer modelling experiments, by site-directed mutagenesis a series of cryptogein variants was prepared with altered abilities to bind sterols, phospholipids or both. The sterol binding and phospholipid transfer activities corresponded well with the previously reported structural data. Induction of the synthesis of reactive oxygen species (ROS) in tobacco cells in suspension and proteomic analysis of intercellular fluid changes in tobacco leaves triggered by these mutant proteins were not proportional to their ability to bind or transfer sterols and phospholipids. However, changes in the intercellular proteome corresponded to transcription levels of defence genes and resistance to P. parasitica and structure-prediction of mutants did not reveal any significant changes in protein structure. These results suggest, contrary to previous proposals, that the sterol-binding ability of cryptogein and its mutants, and the associated conformational change in the ω-loop, might not be principal factors in either ROS production or resistance induction. Nevertheless, the results support the importance of the ω-loop for the interaction of the protein with the high affinity binding site on the plasma membrane.</div>
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<AbstractText>Cryptogein is a proteinaceous elicitor secreted by Phytophthora cryptogea that can induce resistance to P. parasitica in tobacco plants. On the basis of previous computer modelling experiments, by site-directed mutagenesis a series of cryptogein variants was prepared with altered abilities to bind sterols, phospholipids or both. The sterol binding and phospholipid transfer activities corresponded well with the previously reported structural data. Induction of the synthesis of reactive oxygen species (ROS) in tobacco cells in suspension and proteomic analysis of intercellular fluid changes in tobacco leaves triggered by these mutant proteins were not proportional to their ability to bind or transfer sterols and phospholipids. However, changes in the intercellular proteome corresponded to transcription levels of defence genes and resistance to P. parasitica and structure-prediction of mutants did not reveal any significant changes in protein structure. These results suggest, contrary to previous proposals, that the sterol-binding ability of cryptogein and its mutants, and the associated conformational change in the ω-loop, might not be principal factors in either ROS production or resistance induction. Nevertheless, the results support the importance of the ω-loop for the interaction of the protein with the high affinity binding site on the plasma membrane.</AbstractText>
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