Oligandrin. A proteinaceous molecule produced by the mycoparasite Pythium oligandrum induces resistance to Phytophthora parasitica infection in tomato plants.
Identifieur interne : 002810 ( Main/Exploration ); précédent : 002809; suivant : 002811Oligandrin. A proteinaceous molecule produced by the mycoparasite Pythium oligandrum induces resistance to Phytophthora parasitica infection in tomato plants.
Auteurs : K. Picard [France] ; M. Ponchet ; J P Blein ; P. Rey ; Y. Tirilly ; N. BenhamouSource :
- Plant physiology [ 0032-0889 ] ; 2000.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Analyse de séquence de protéine (MeSH), Chromatographie en phase liquide à haute performance (MeSH), Données de séquences moléculaires (MeSH), Lycopersicon esculentum (microbiologie), Lycopersicon esculentum (ultrastructure), Maladies des plantes (microbiologie), Microscopie électronique (MeSH), Or colloïdal (MeSH), Phytophthora (pathogénicité), Protéines d'algue (composition chimique), Protéines d'algue (isolement et purification), Protéines d'algue (pharmacologie), Protéines de transport (MeSH), Protéines et peptides de signalisation intercellulaire (MeSH), Protéines fongiques (composition chimique), Protéines fongiques (isolement et purification), Protéines fongiques (pharmacologie), Pythium (composition chimique), Structures de plante (microbiologie), Structures de plante (ultrastructure), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Protéines d'algue, Protéines fongiques, Pythium.
- isolement et purification : Protéines d'algue, Protéines fongiques.
- microbiologie : Lycopersicon esculentum, Maladies des plantes, Structures de plante.
- pathogénicité : Phytophthora.
- pharmacologie : Protéines d'algue, Protéines fongiques.
- ultrastructure : Alignement de séquences, Analyse de séquence de protéine, Chromatographie en phase liquide à haute performance, Données de séquences moléculaires, Lycopersicon esculentum, Microscopie électronique, Or colloïdal, Protéines de transport, Protéines et peptides de signalisation intercellulaire, Structures de plante, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Algal Proteins (chemistry), Algal Proteins (isolation & purification), Algal Proteins (pharmacology), Amino Acid Sequence (MeSH), Carrier Proteins (MeSH), Chromatography, High Pressure Liquid (MeSH), Fungal Proteins (chemistry), Fungal Proteins (isolation & purification), Fungal Proteins (pharmacology), Gold Colloid (MeSH), Intercellular Signaling Peptides and Proteins (MeSH), Lycopersicon esculentum (microbiology), Lycopersicon esculentum (ultrastructure), Microscopy, Electron (MeSH), Molecular Sequence Data (MeSH), Phytophthora (pathogenicity), Plant Diseases (microbiology), Plant Structures (microbiology), Plant Structures (ultrastructure), Pythium (chemistry), Sequence Alignment (MeSH), Sequence Analysis, Protein (MeSH).
- MESH :
- chemical , chemistry : Algal Proteins, Fungal Proteins.
- chemical , isolation & purification : Algal Proteins, Fungal Proteins.
- chemical , pharmacology : Algal Proteins, Fungal Proteins.
- chemistry : Pythium.
- microbiology : Lycopersicon esculentum, Plant Diseases, Plant Structures.
- pathogenicity : Phytophthora.
- ultrastructure : Lycopersicon esculentum, Plant Structures.
- Amino Acid Sequence, Carrier Proteins, Chromatography, High Pressure Liquid, Gold Colloid, Intercellular Signaling Peptides and Proteins, Microscopy, Electron, Molecular Sequence Data, Sequence Alignment, Sequence Analysis, Protein.
Abstract
A low-molecular weight protein, termed oligandrin, was purified to homogeneity from the culture filtrate of the mycoparasitic fungus Pythium oligandrum. When applied to decapitated tomato (Lycopersicon esculentum Mill. var. Prisca) plants, this protein displayed the ability to induce plant defense reactions that contributed to restrict stem cell invasion by the pathogenic fungus Phytophthora parasitica. According to its N-terminal sequence, low-molecular weight, acidic isoelectric point, ultraviolet spectrum, and migration profile, the P. oligandrum-produced oligandrin was found to share some similarities with several elicitins from other Phytophthora spp. and Pythium spp. However, oligandrin did not induce hypersensitive reactions. A significant decrease in disease incidence was monitored in oligandrin-treated plants as compared with water-treated plants. Ultrastructural investigations of the infected tomato stem tissues from non-treated plants showed a rapid colonization of all tissues associated with a marked host cell disorganization. In stems from oligandrin-treated plants, restriction of fungal growth to the outermost tissues and decrease in pathogen viability were the main features of the host-pathogen interaction. Invading fungal cells were markedly damaged at a time when the cellulose component of their cell walls was quite well preserved. Host reactions included the plugging of intercellular spaces as well as the occasional formation of wall appositions at sites of potential pathogen entry. In addition, pathogen ingress in the epidermis was associated with the deposition of an electron-opaque material in most invaded intercellular spaces. This material, lining the primary walls, usually extended toward the inside to form deposits that frequently interacted with the wall of invading hyphae. In the absence of fungal challenge, host reactions were not detected.
DOI: 10.1104/pp.124.1.379
PubMed: 10982451
PubMed Central: PMC59151
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Picard</name><affiliation wicri:level="3"><nlm:affiliation>Laboratoire de Microbiologie et Sécurité Alimentaire, Université de Brest, Technopôle Brest-Iroise, 29200 Plouzané, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Microbiologie et Sécurité Alimentaire, Université de Brest, Technopôle Brest-Iroise, 29200 Plouzané</wicri:regionArea><placeName><region type="region" nuts="2">Région Bretagne</region><settlement type="city">Plouzané</settlement></placeName></affiliation></author><author><name sortKey="Ponchet, M" sort="Ponchet, M" uniqKey="Ponchet M" first="M" last="Ponchet">M. Ponchet</name></author><author><name sortKey="Blein, J P" sort="Blein, J P" uniqKey="Blein J" first="J P" last="Blein">J P Blein</name></author><author><name sortKey="Rey, P" sort="Rey, P" uniqKey="Rey P" first="P" last="Rey">P. Rey</name></author><author><name sortKey="Tirilly, Y" sort="Tirilly, Y" uniqKey="Tirilly Y" first="Y" last="Tirilly">Y. 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(pathogenicity)</term><term>Plant Diseases (microbiology)</term><term>Plant Structures (microbiology)</term><term>Plant Structures (ultrastructure)</term><term>Pythium (chemistry)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Analysis, Protein (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Analyse de séquence de protéine (MeSH)</term><term>Chromatographie en phase liquide à haute performance (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Lycopersicon esculentum (microbiologie)</term><term>Lycopersicon esculentum (ultrastructure)</term><term>Maladies des plantes (microbiologie)</term><term>Microscopie électronique (MeSH)</term><term>Or colloïdal (MeSH)</term><term>Phytophthora (pathogénicité)</term><term>Protéines d'algue (composition chimique)</term><term>Protéines d'algue (isolement et purification)</term><term>Protéines d'algue (pharmacologie)</term><term>Protéines de transport 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scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines d'algue</term><term>Protéines fongiques</term><term>Pythium</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines d'algue</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Lycopersicon esculentum</term><term>Maladies des plantes</term><term>Structures de plante</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Lycopersicon esculentum</term><term>Plant Diseases</term><term>Plant Structures</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Phytophthora</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Phytophthora</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Protéines d'algue</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Lycopersicon esculentum</term><term>Plant Structures</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Carrier Proteins</term><term>Chromatography, High Pressure Liquid</term><term>Gold Colloid</term><term>Intercellular Signaling Peptides and Proteins</term><term>Microscopy, Electron</term><term>Molecular Sequence Data</term><term>Sequence Alignment</term><term>Sequence Analysis, Protein</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Alignement de séquences</term><term>Analyse de séquence de protéine</term><term>Chromatographie en phase liquide à haute performance</term><term>Données de séquences moléculaires</term><term>Lycopersicon esculentum</term><term>Microscopie électronique</term><term>Or colloïdal</term><term>Protéines de transport</term><term>Protéines et peptides de signalisation intercellulaire</term><term>Structures de plante</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A low-molecular weight protein, termed oligandrin, was purified to homogeneity from the culture filtrate of the mycoparasitic fungus Pythium oligandrum. When applied to decapitated tomato (Lycopersicon esculentum Mill. var. Prisca) plants, this protein displayed the ability to induce plant defense reactions that contributed to restrict stem cell invasion by the pathogenic fungus Phytophthora parasitica. According to its N-terminal sequence, low-molecular weight, acidic isoelectric point, ultraviolet spectrum, and migration profile, the P. oligandrum-produced oligandrin was found to share some similarities with several elicitins from other Phytophthora spp. and Pythium spp. However, oligandrin did not induce hypersensitive reactions. A significant decrease in disease incidence was monitored in oligandrin-treated plants as compared with water-treated plants. Ultrastructural investigations of the infected tomato stem tissues from non-treated plants showed a rapid colonization of all tissues associated with a marked host cell disorganization. In stems from oligandrin-treated plants, restriction of fungal growth to the outermost tissues and decrease in pathogen viability were the main features of the host-pathogen interaction. Invading fungal cells were markedly damaged at a time when the cellulose component of their cell walls was quite well preserved. Host reactions included the plugging of intercellular spaces as well as the occasional formation of wall appositions at sites of potential pathogen entry. In addition, pathogen ingress in the epidermis was associated with the deposition of an electron-opaque material in most invaded intercellular spaces. This material, lining the primary walls, usually extended toward the inside to form deposits that frequently interacted with the wall of invading hyphae. In the absence of fungal challenge, host reactions were not detected.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10982451</PMID><DateCompleted><Year>2000</Year><Month>11</Month><Day>24</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>124</Volume><Issue>1</Issue><PubDate><Year>2000</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Oligandrin. A proteinaceous molecule produced by the mycoparasite Pythium oligandrum induces resistance to Phytophthora parasitica infection in tomato plants.</ArticleTitle><Pagination><MedlinePgn>379-95</MedlinePgn></Pagination><Abstract><AbstractText>A low-molecular weight protein, termed oligandrin, was purified to homogeneity from the culture filtrate of the mycoparasitic fungus Pythium oligandrum. When applied to decapitated tomato (Lycopersicon esculentum Mill. var. Prisca) plants, this protein displayed the ability to induce plant defense reactions that contributed to restrict stem cell invasion by the pathogenic fungus Phytophthora parasitica. According to its N-terminal sequence, low-molecular weight, acidic isoelectric point, ultraviolet spectrum, and migration profile, the P. oligandrum-produced oligandrin was found to share some similarities with several elicitins from other Phytophthora spp. and Pythium spp. However, oligandrin did not induce hypersensitive reactions. A significant decrease in disease incidence was monitored in oligandrin-treated plants as compared with water-treated plants. Ultrastructural investigations of the infected tomato stem tissues from non-treated plants showed a rapid colonization of all tissues associated with a marked host cell disorganization. In stems from oligandrin-treated plants, restriction of fungal growth to the outermost tissues and decrease in pathogen viability were the main features of the host-pathogen interaction. Invading fungal cells were markedly damaged at a time when the cellulose component of their cell walls was quite well preserved. Host reactions included the plugging of intercellular spaces as well as the occasional formation of wall appositions at sites of potential pathogen entry. In addition, pathogen ingress in the epidermis was associated with the deposition of an electron-opaque material in most invaded intercellular spaces. This material, lining the primary walls, usually extended toward the inside to form deposits that frequently interacted with the wall of invading hyphae. In the absence of fungal challenge, host reactions were not detected.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Picard</LastName><ForeName>K</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Laboratoire de Microbiologie et Sécurité Alimentaire, Université de Brest, Technopôle Brest-Iroise, 29200 Plouzané, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ponchet</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Blein</LastName><ForeName>J P</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Rey</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Tirilly</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Benhamou</LastName><ForeName>N</ForeName><Initials>N</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Physiol</MedlineTA><NlmUniqueID>0401224</NlmUniqueID><ISSNLinking>0032-0889</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020418">Algal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017979">Gold Colloid</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D036341">Intercellular Signaling Peptides and Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C415980">Oligandrin protein, Pythium oligandrum</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020418" MajorTopicYN="N">Algal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="Y">Carrier Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017979" MajorTopicYN="N">Gold Colloid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D036341" MajorTopicYN="N">Intercellular Signaling Peptides and Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018551" MajorTopicYN="N">Lycopersicon esculentum</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008854" MajorTopicYN="N">Microscopy, Electron</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName><QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018514" MajorTopicYN="N">Plant Structures</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011775" MajorTopicYN="N">Pythium</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020539" MajorTopicYN="N">Sequence Analysis, Protein</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>9</Month><Day>12</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>2</Month><Day>28</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>9</Month><Day>12</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10982451</ArticleId><ArticleId IdType="pmc">PMC59151</ArticleId><ArticleId IdType="doi">10.1104/pp.124.1.379</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Plant Physiol. 1995 Nov;109(3):1025-1031</Citation><ArticleIdList><ArticleId IdType="pubmed">12228650</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1985 Mar;77(3):544-51</Citation><ArticleIdList><ArticleId 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Benhamou</name><name sortKey="Blein, J P" sort="Blein, J P" uniqKey="Blein J" first="J P" last="Blein">J P Blein</name><name sortKey="Ponchet, M" sort="Ponchet, M" uniqKey="Ponchet M" first="M" last="Ponchet">M. Ponchet</name><name sortKey="Rey, P" sort="Rey, P" uniqKey="Rey P" first="P" last="Rey">P. Rey</name><name sortKey="Tirilly, Y" sort="Tirilly, Y" uniqKey="Tirilly Y" first="Y" last="Tirilly">Y. Tirilly</name></noCountry><country name="France"><region name="Région Bretagne"><name sortKey="Picard, K" sort="Picard, K" uniqKey="Picard K" first="K" last="Picard">K. Picard</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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