PhytophthoraV1, Main, Exploration, bibRecord, 000902

The plant defense and pathogen counterdefense mediated by Hevea brasiliensis serine protease HbSPA and Phytophthora palmivora extracellular protease inhibitor PpEPI10.

Identifieur interne : 000902 ( Main/Exploration ); précédent : 000901; suivant : 000903

The plant defense and pathogen counterdefense mediated by Hevea brasiliensis serine protease HbSPA and Phytophthora palmivora extracellular protease inhibitor PpEPI10.

Auteurs : Kitiya Ekchaweng [Thaïlande, États-Unis] ; Edouard Evangelisti [Royaume-Uni] ; Sebastian Schornack [Royaume-Uni] ; Miaoying Tian [États-Unis] ; Nunta Churngchow [Thaïlande]

Source :

PloS one [ 1932-6203 ] ; 2017.

RBID : pubmed:28459807

Descripteurs français

English descriptors

KwdEn :
- Chromatography, Affinity (MeSH), Disease Resistance (physiology), Escherichia coli (MeSH), Gene Transfer Techniques (MeSH), Hevea (enzymology), Hevea (genetics), Hevea (parasitology), Host-Pathogen Interactions (MeSH), Immunoprecipitation (MeSH), Organisms, Genetically Modified (MeSH), Phytophthora (genetics), Phytophthora (metabolism), Plant Proteins (genetics), Plant Proteins (metabolism), Polymerase Chain Reaction (MeSH), Protease Inhibitors (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Serine Proteases (genetics), Serine Proteases (metabolism), Tobacco (genetics), Tobacco (metabolism).
MESH :
- chemical , genetics : Plant Proteins, Recombinant Proteins, Serine Proteases.
- enzymology : Hevea.
- genetics : Hevea, Phytophthora, Tobacco.
- metabolism : Phytophthora, Plant Proteins, Protease Inhibitors, Recombinant Proteins, Serine Proteases, Tobacco.
- parasitology : Hevea.
- physiology : Disease Resistance.
- Chromatography, Affinity, Escherichia coli, Gene Transfer Techniques, Host-Pathogen Interactions, Immunoprecipitation, Organisms, Genetically Modified, Polymerase Chain Reaction.

Abstract

Rubber tree (Hevea brasiliensis Muell. Arg) is an important economic crop in Thailand. Leaf fall and black stripe diseases caused by the aggressive oomycete pathogen Phytophthora palmivora, cause deleterious damage on rubber tree growth leading to decrease of latex production. To gain insights into the molecular function of H. brasiliensis subtilisin-like serine proteases, the HbSPA, HbSPB, and HbSPC genes were transiently expressed in Nicotiana benthamiana via agroinfiltration. A functional protease encoded by HbSPA was successfully expressed in the apoplast of N. benthamiana leaves. Transient expression of HbSPA in N. benthamiana leaves enhanced resistance to P. palmivora, suggesting that HbSPA plays an important role in plant defense. P. palmivora Kazal-like extracellular protease inhibitor 10 (PpEPI10), an apoplastic effector, has been implicated in pathogenicity through the suppression of H. brasiliensis protease. Semi-quantitative RT-PCR revealed that the PpEPI10 gene was significantly up-regulated during colonization of rubber tree by P. palmivora. Concurrently, the HbSPA gene was highly expressed during infection. To investigate a possible interaction between HbSPA and PpEPI10, the recombinant PpEPI10 protein (rPpEPI10) was expressed in Escherichia coli and purified using affinity chromatography. In-gel zymogram and co-immunoprecipitation (co-IP) assays demonstrated that rPpEPI10 specifically inhibited and interacted with HbSPA. The targeting of HbSPA by PpEPI10 revealed a defense-counterdefense mechanism, which is mediated by plant protease and pathogen protease inhibitor, in H. brasiliensis-P. palmivora interactions.

DOI: 10.1371/journal.pone.0175795
PubMed: 28459807
PubMed Central: PMC5411025

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000982
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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography, Affinity (MeSH)</term>
<term>Disease Resistance (physiology)</term>
<term>Escherichia coli (MeSH)</term>
<term>Gene Transfer Techniques (MeSH)</term>
<term>Hevea (enzymology)</term>
<term>Hevea (genetics)</term>
<term>Hevea (parasitology)</term>
<term>Host-Pathogen Interactions (MeSH)</term>
<term>Immunoprecipitation (MeSH)</term>
<term>Organisms, Genetically Modified (MeSH)</term>
<term>Phytophthora (genetics)</term>
<term>Phytophthora (metabolism)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Polymerase Chain Reaction (MeSH)</term>
<term>Protease Inhibitors (metabolism)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Serine Proteases (genetics)</term>
<term>Serine Proteases (metabolism)</term>
<term>Tobacco (genetics)</term>
<term>Tobacco (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie d'affinité (MeSH)</term>
<term>Escherichia coli (MeSH)</term>
<term>Hevea (enzymologie)</term>
<term>Hevea (génétique)</term>
<term>Hevea (parasitologie)</term>
<term>Immunoprécipitation (MeSH)</term>
<term>Inhibiteurs de protéases (métabolisme)</term>
<term>Interactions hôte-pathogène (MeSH)</term>
<term>Organismes génétiquement modifiés (MeSH)</term>
<term>Phytophthora (génétique)</term>
<term>Phytophthora (métabolisme)</term>
<term>Protéases à sérine (génétique)</term>
<term>Protéases à sérine (métabolisme)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Réaction de polymérisation en chaîne (MeSH)</term>
<term>Résistance à la maladie (physiologie)</term>
<term>Tabac (génétique)</term>
<term>Tabac (métabolisme)</term>
<term>Techniques de transfert de gènes (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Plant Proteins</term>
<term>Recombinant Proteins</term>
<term>Serine Proteases</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Hevea</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Hevea</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Hevea</term>
<term>Phytophthora</term>
<term>Tobacco</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Hevea</term>
<term>Phytophthora</term>
<term>Protéases à sérine</term>
<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
<term>Tabac</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phytophthora</term>
<term>Plant Proteins</term>
<term>Protease Inhibitors</term>
<term>Recombinant Proteins</term>
<term>Serine Proteases</term>
<term>Tobacco</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Inhibiteurs de protéases</term>
<term>Phytophthora</term>
<term>Protéases à sérine</term>
<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
<term>Tabac</term>
</keywords>
<keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Hevea</term>
</keywords>
<keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Hevea</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Résistance à la maladie</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Disease Resistance</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Chromatography, Affinity</term>
<term>Escherichia coli</term>
<term>Gene Transfer Techniques</term>
<term>Host-Pathogen Interactions</term>
<term>Immunoprecipitation</term>
<term>Organisms, Genetically Modified</term>
<term>Polymerase Chain Reaction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Chromatographie d'affinité</term>
<term>Escherichia coli</term>
<term>Immunoprécipitation</term>
<term>Interactions hôte-pathogène</term>
<term>Organismes génétiquement modifiés</term>
<term>Réaction de polymérisation en chaîne</term>
<term>Techniques de transfert de gènes</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Rubber tree (Hevea brasiliensis Muell. Arg) is an important economic crop in Thailand. Leaf fall and black stripe diseases caused by the aggressive oomycete pathogen Phytophthora palmivora, cause deleterious damage on rubber tree growth leading to decrease of latex production. To gain insights into the molecular function of H. brasiliensis subtilisin-like serine proteases, the HbSPA, HbSPB, and HbSPC genes were transiently expressed in Nicotiana benthamiana via agroinfiltration. A functional protease encoded by HbSPA was successfully expressed in the apoplast of N. benthamiana leaves. Transient expression of HbSPA in N. benthamiana leaves enhanced resistance to P. palmivora, suggesting that HbSPA plays an important role in plant defense. P. palmivora Kazal-like extracellular protease inhibitor 10 (PpEPI10), an apoplastic effector, has been implicated in pathogenicity through the suppression of H. brasiliensis protease. Semi-quantitative RT-PCR revealed that the PpEPI10 gene was significantly up-regulated during colonization of rubber tree by P. palmivora. Concurrently, the HbSPA gene was highly expressed during infection. To investigate a possible interaction between HbSPA and PpEPI10, the recombinant PpEPI10 protein (rPpEPI10) was expressed in Escherichia coli and purified using affinity chromatography. In-gel zymogram and co-immunoprecipitation (co-IP) assays demonstrated that rPpEPI10 specifically inhibited and interacted with HbSPA. The targeting of HbSPA by PpEPI10 revealed a defense-counterdefense mechanism, which is mediated by plant protease and pathogen protease inhibitor, in H. brasiliensis-P. palmivora interactions.</div>
</front>
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<ArticleTitle>The plant defense and pathogen counterdefense mediated by Hevea brasiliensis serine protease HbSPA and Phytophthora palmivora extracellular protease inhibitor PpEPI10.</ArticleTitle>
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<Abstract><AbstractText>Rubber tree (Hevea brasiliensis Muell. Arg) is an important economic crop in Thailand. Leaf fall and black stripe diseases caused by the aggressive oomycete pathogen Phytophthora palmivora, cause deleterious damage on rubber tree growth leading to decrease of latex production. To gain insights into the molecular function of H. brasiliensis subtilisin-like serine proteases, the HbSPA, HbSPB, and HbSPC genes were transiently expressed in Nicotiana benthamiana via agroinfiltration. A functional protease encoded by HbSPA was successfully expressed in the apoplast of N. benthamiana leaves. Transient expression of HbSPA in N. benthamiana leaves enhanced resistance to P. palmivora, suggesting that HbSPA plays an important role in plant defense. P. palmivora Kazal-like extracellular protease inhibitor 10 (PpEPI10), an apoplastic effector, has been implicated in pathogenicity through the suppression of H. brasiliensis protease. Semi-quantitative RT-PCR revealed that the PpEPI10 gene was significantly up-regulated during colonization of rubber tree by P. palmivora. Concurrently, the HbSPA gene was highly expressed during infection. To investigate a possible interaction between HbSPA and PpEPI10, the recombinant PpEPI10 protein (rPpEPI10) was expressed in Escherichia coli and purified using affinity chromatography. In-gel zymogram and co-immunoprecipitation (co-IP) assays demonstrated that rPpEPI10 specifically inhibited and interacted with HbSPA. The targeting of HbSPA by PpEPI10 revealed a defense-counterdefense mechanism, which is mediated by plant protease and pathogen protease inhibitor, in H. brasiliensis-P. palmivora interactions.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ekchaweng</LastName>
<ForeName>Kitiya</ForeName>
<Initials>K</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0001-6735-2893</Identifier>
<AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Science, Prince of Songkla University, Hat Yai, Songkhla, Thailand.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Plant and Environmental Protection Sciences, University of Hawaii at Manoa, Honolulu, Hawaii, United States of America.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>East-West Center, Honolulu, Hawaii, United States of America.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Evangelisti</LastName>
<ForeName>Edouard</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Sainsbury Laboratory Cambridge University, Cambridge, United Kingdom.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Schornack</LastName>
<ForeName>Sebastian</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Sainsbury Laboratory Cambridge University, Cambridge, United Kingdom.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tian</LastName>
<ForeName>Miaoying</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Plant and Environmental Protection Sciences, University of Hawaii at Manoa, Honolulu, Hawaii, United States of America.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Churngchow</LastName>
<ForeName>Nunta</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Science, Prince of Songkla University, Hat Yai, Songkhla, Thailand.</Affiliation>
</AffiliationInfo>
</Author>
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<Language>eng</Language>
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<Month>05</Month>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>EC 3.4.-</RegistryNumber>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D002846" MajorTopicYN="N">Chromatography, Affinity</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D060467" MajorTopicYN="N">Disease Resistance</DescriptorName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName>
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<MeshHeading><DescriptorName UI="D018014" MajorTopicYN="N">Gene Transfer Techniques</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D028482" MajorTopicYN="N">Hevea</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054884" MajorTopicYN="Y">Host-Pathogen Interactions</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D047468" MajorTopicYN="N">Immunoprecipitation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D030781" MajorTopicYN="N">Organisms, Genetically Modified</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
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The plant defense and pathogen counterdefense mediated by Hevea brasiliensis serine protease HbSPA and Phytophthora palmivora extracellular protease inhibitor PpEPI10.

The plant defense and pathogen counterdefense mediated by Hevea brasiliensis serine protease HbSPA and Phytophthora palmivora extracellular protease inhibitor PpEPI10.

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