A new family of plant antifungal proteins.
Identifieur interne : 000522 ( Main/Exploration ); précédent : 000521; suivant : 000523A new family of plant antifungal proteins.
Auteurs : A J Vigers ; W K Roberts ; C P SelitrennikoffSource :
- Molecular plant-microbe interactions : MPMI [ 0894-0282 ]
Descripteurs français
- KwdFr :
- Antifongiques (composition chimique), Antifongiques (isolement et purification), Antifongiques (pharmacologie), Candida albicans (effets des médicaments et des substances chimiques), Données de séquences moléculaires (MeSH), Graines (composition chimique), Immunotransfert (MeSH), Inhibiteurs trypsiques (MeSH), Plantes (composition chimique), Protéines végétales (composition chimique), Protéines végétales (isolement et purification), Protéines végétales (pharmacologie), Réactions croisées (MeSH), Séquence d'acides aminés (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- composition chimique : Antifongiques, Graines, Plantes, Protéines végétales.
- effets des médicaments et des substances chimiques : Candida albicans.
- isolement et purification : Antifongiques, Protéines végétales.
- pharmacologie : Antifongiques, Protéines végétales.
- Données de séquences moléculaires, Immunotransfert, Inhibiteurs trypsiques, Réactions croisées, Séquence d'acides aminés, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Antifungal Agents (chemistry), Antifungal Agents (isolation & purification), Antifungal Agents (pharmacology), Candida albicans (drug effects), Cross Reactions (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Immunoblotting (MeSH), Molecular Sequence Data (MeSH), Plant Proteins (chemistry), Plant Proteins (isolation & purification), Plant Proteins (pharmacology), Plants (chemistry), Seeds (chemistry), Trypsin Inhibitors (MeSH).
- MESH :
- chemical , chemistry : Antifungal Agents, Plant Proteins.
- chemical , isolation & purification : Antifungal Agents, Plant Proteins.
- chemical , pharmacology : Antifungal Agents, Plant Proteins.
- chemistry : Plants, Seeds.
- drug effects : Candida albicans.
- Amino Acid Sequence, Cross Reactions, Electrophoresis, Polyacrylamide Gel, Immunoblotting, Molecular Sequence Data, Trypsin Inhibitors.
Abstract
Plant seeds contain high concentrations of many antimicrobial proteins. These include chitinases, beta-1,3-glucanases, proteinase inhibitors, and ribosome-inactivating proteins. We recently reported the presence in corn seeds of zeamatin, a protein that has potent activity against a variety of fungi but has none of the above activities. Zeamatin is a 22-kDa protein that acts by causing membrane permeabilization Using a novel bioautography technique, we found similar antifungal proteins in the seeds of 6 of 12 plants examined. A polyclonal antiserum was raised against zeamatin and was used in immunoblots to confirm the presence of zeamatinlike proteins in these seeds. N-terminal amino acid sequencing was carried out on the antifungal proteins from corn, oats, sorghum, and wheat, and these sequences revealed considerable homology with each other. Interestingly, these N-terminal sequences are also similar to those of thaumatin, a pathogenesis-related protein from tobacco, and two salt stress-induced proteins. These results indicate that zeamatin is not unique but is a member of a previously unrecognized family of plant defense proteins that may include some species of pathogenesis-related proteins.
DOI: 10.1094/mpmi-4-315
PubMed: 1799695
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A new family of plant antifungal proteins.</title><author><name sortKey="Vigers, A J" sort="Vigers, A J" uniqKey="Vigers A" first="A J" last="Vigers">A J Vigers</name><affiliation><nlm:affiliation>Department of Cellular and Structural Biology, University of Colorado Health Sciences Center, Denver 80262 U.S.A.</nlm:affiliation><wicri:noCountry code="subField">Denver 80262 U.S.A.</wicri:noCountry></affiliation></author><author><name sortKey="Roberts, W K" sort="Roberts, W K" uniqKey="Roberts W" first="W K" last="Roberts">W K Roberts</name></author><author><name sortKey="Selitrennikoff, C P" sort="Selitrennikoff, C P" uniqKey="Selitrennikoff C" first="C P" last="Selitrennikoff">C P Selitrennikoff</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991 Jul-Aug</date><idno type="RBID">pubmed:1799695</idno><idno type="pmid">1799695</idno><idno type="doi">10.1094/mpmi-4-315</idno><idno type="wicri:Area/Main/Corpus">000527</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000527</idno><idno type="wicri:Area/Main/Curation">000527</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000527</idno><idno type="wicri:Area/Main/Exploration">000527</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A new family of plant antifungal proteins.</title><author><name sortKey="Vigers, A J" sort="Vigers, A J" uniqKey="Vigers A" first="A J" last="Vigers">A J Vigers</name><affiliation><nlm:affiliation>Department of Cellular and Structural Biology, University of Colorado Health Sciences Center, Denver 80262 U.S.A.</nlm:affiliation><wicri:noCountry code="subField">Denver 80262 U.S.A.</wicri:noCountry></affiliation></author><author><name sortKey="Roberts, W K" sort="Roberts, W K" uniqKey="Roberts W" first="W K" last="Roberts">W K Roberts</name></author><author><name sortKey="Selitrennikoff, C P" sort="Selitrennikoff, C P" uniqKey="Selitrennikoff C" first="C P" last="Selitrennikoff">C P Selitrennikoff</name></author></analytic><series><title level="j">Molecular plant-microbe interactions : MPMI</title><idno type="ISSN">0894-0282</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Antifungal Agents (chemistry)</term><term>Antifungal Agents (isolation & purification)</term><term>Antifungal Agents (pharmacology)</term><term>Candida albicans (drug effects)</term><term>Cross Reactions (MeSH)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Immunoblotting (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (isolation & purification)</term><term>Plant Proteins (pharmacology)</term><term>Plants (chemistry)</term><term>Seeds (chemistry)</term><term>Trypsin Inhibitors (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antifongiques (composition chimique)</term><term>Antifongiques (isolement et purification)</term><term>Antifongiques (pharmacologie)</term><term>Candida albicans (effets des médicaments et des substances chimiques)</term><term>Données de séquences moléculaires (MeSH)</term><term>Graines (composition chimique)</term><term>Immunotransfert (MeSH)</term><term>Inhibiteurs trypsiques (MeSH)</term><term>Plantes (composition chimique)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (isolement et purification)</term><term>Protéines végétales (pharmacologie)</term><term>Réactions croisées (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antifungal Agents</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Antifungal Agents</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antifungal Agents</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Plants</term><term>Seeds</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Antifongiques</term><term>Graines</term><term>Plantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Candida albicans</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Candida albicans</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Antifongiques</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antifongiques</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cross Reactions</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Immunoblotting</term><term>Molecular Sequence Data</term><term>Trypsin Inhibitors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Immunotransfert</term><term>Inhibiteurs trypsiques</term><term>Réactions croisées</term><term>Séquence d'acides aminés</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Plant seeds contain high concentrations of many antimicrobial proteins. These include chitinases, beta-1,3-glucanases, proteinase inhibitors, and ribosome-inactivating proteins. We recently reported the presence in corn seeds of zeamatin, a protein that has potent activity against a variety of fungi but has none of the above activities. Zeamatin is a 22-kDa protein that acts by causing membrane permeabilization Using a novel bioautography technique, we found similar antifungal proteins in the seeds of 6 of 12 plants examined. A polyclonal antiserum was raised against zeamatin and was used in immunoblots to confirm the presence of zeamatinlike proteins in these seeds. N-terminal amino acid sequencing was carried out on the antifungal proteins from corn, oats, sorghum, and wheat, and these sequences revealed considerable homology with each other. Interestingly, these N-terminal sequences are also similar to those of thaumatin, a pathogenesis-related protein from tobacco, and two salt stress-induced proteins. These results indicate that zeamatin is not unique but is a member of a previously unrecognized family of plant defense proteins that may include some species of pathogenesis-related proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1799695</PMID><DateCompleted><Year>1992</Year><Month>04</Month><Day>20</Day></DateCompleted><DateRevised><Year>2019</Year><Month>10</Month><Day>28</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0894-0282</ISSN><JournalIssue CitedMedium="Print"><Volume>4</Volume><Issue>4</Issue><PubDate><MedlineDate>1991 Jul-Aug</MedlineDate></PubDate></JournalIssue><Title>Molecular plant-microbe interactions : MPMI</Title><ISOAbbreviation>Mol Plant Microbe Interact</ISOAbbreviation></Journal><ArticleTitle>A new family of plant antifungal proteins.</ArticleTitle><Pagination><MedlinePgn>315-23</MedlinePgn></Pagination><Abstract><AbstractText>Plant seeds contain high concentrations of many antimicrobial proteins. These include chitinases, beta-1,3-glucanases, proteinase inhibitors, and ribosome-inactivating proteins. We recently reported the presence in corn seeds of zeamatin, a protein that has potent activity against a variety of fungi but has none of the above activities. Zeamatin is a 22-kDa protein that acts by causing membrane permeabilization Using a novel bioautography technique, we found similar antifungal proteins in the seeds of 6 of 12 plants examined. A polyclonal antiserum was raised against zeamatin and was used in immunoblots to confirm the presence of zeamatinlike proteins in these seeds. N-terminal amino acid sequencing was carried out on the antifungal proteins from corn, oats, sorghum, and wheat, and these sequences revealed considerable homology with each other. Interestingly, these N-terminal sequences are also similar to those of thaumatin, a pathogenesis-related protein from tobacco, and two salt stress-induced proteins. These results indicate that zeamatin is not unique but is a member of a previously unrecognized family of plant defense proteins that may include some species of pathogenesis-related proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vigers</LastName><ForeName>A J</ForeName><Initials>AJ</Initials><AffiliationInfo><Affiliation>Department of Cellular and Structural Biology, University of Colorado Health Sciences Center, Denver 80262 U.S.A.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Roberts</LastName><ForeName>W K</ForeName><Initials>WK</Initials></Author><Author ValidYN="Y"><LastName>Selitrennikoff</LastName><ForeName>C P</ForeName><Initials>CP</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>Mol Plant Microbe Interact</MedlineTA><NlmUniqueID>9107902</NlmUniqueID><ISSNLinking>0894-0282</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000935">Antifungal Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014361">Trypsin Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>130590-19-1</RegistryNumber><NameOfSubstance UI="C073468">zeamatin protein, Zea mays</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000935" MajorTopicYN="N">Antifungal Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002176" MajorTopicYN="N">Candida albicans</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003429" MajorTopicYN="N">Cross Reactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015151" MajorTopicYN="N">Immunoblotting</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012639" MajorTopicYN="N">Seeds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014361" MajorTopicYN="Y">Trypsin Inhibitors</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>7</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>7</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>7</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1799695</ArticleId><ArticleId IdType="doi">10.1094/mpmi-4-315</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Roberts, W K" sort="Roberts, W K" uniqKey="Roberts W" first="W K" last="Roberts">W K Roberts</name><name sortKey="Selitrennikoff, C P" sort="Selitrennikoff, C P" uniqKey="Selitrennikoff C" first="C P" last="Selitrennikoff">C P Selitrennikoff</name><name sortKey="Vigers, A J" sort="Vigers, A J" uniqKey="Vigers A" first="A J" last="Vigers">A J Vigers</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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