A P-Glycoprotein Is Linked to Resistance to the Bacillus thuringiensis Cry3Aa Toxin in a Leaf Beetle.
Identifieur interne : 001A30 ( Main/Exploration ); précédent : 001A29; suivant : 001A31A P-Glycoprotein Is Linked to Resistance to the Bacillus thuringiensis Cry3Aa Toxin in a Leaf Beetle.
Auteurs : Yannick Pauchet [Allemagne] ; Anne Bretschneider [Allemagne] ; Sylvie Augustin [France] ; David G. Heckel [Allemagne]Source :
- Toxins [ 2072-6651 ] ; 2016.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Coléoptères (effets des médicaments et des substances chimiques), Coléoptères (génétique), Endotoxines (toxicité), Femelle (MeSH), Hémolysines (toxicité), Lignée cellulaire (MeSH), Mâle (MeSH), Protéines bactériennes (toxicité), Résistance aux insecticides (génétique), Sous-famille B de transporteurs à cassette liant l'ATP (génétique).
- MESH :
- effets des médicaments et des substances chimiques : Coléoptères.
- génétique : Coléoptères, Résistance aux insecticides, Sous-famille B de transporteurs à cassette liant l'ATP.
- toxicité : Endotoxines, Hémolysines, Protéines bactériennes.
- Animaux, Femelle, Lignée cellulaire, Mâle.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : ATP Binding Cassette Transporter, Subfamily B.
- chemical , toxicity : Bacterial Proteins, Endotoxins, Hemolysin Proteins.
- drug effects : Coleoptera.
- genetics : Coleoptera, Insecticide Resistance.
- Animals, Cell Line, Female, Male.
Abstract
Chrysomela tremula is a polyvoltine oligophagous leaf beetle responsible for massive attacks on poplar trees. This beetle is an important model for understanding mechanisms of resistance to Bacillus thuringiensis (Bt) insecticidal toxins, because a resistant C. tremula strain has been found that can survive and reproduce on transgenic poplar trees expressing high levels of the Cry3Aa Bt toxin. Resistance to Cry3Aa in this strain is recessive and is controlled by a single autosomal locus. We used a larval midgut transcriptome for C. tremula to search for candidate resistance genes. We discovered a mutation in an ABC protein, member of the B subfamily homologous to P-glycoprotein, which is genetically linked to Cry3Aa resistance in C. tremula. Cultured insect cells heterologously expressing this ABC protein swell and lyse when incubated with Cry3Aa toxin. In light of previous findings in Lepidoptera implicating A subfamily ABC proteins as receptors for Cry2A toxins and C subfamily proteins as receptors for Cry1A and Cry1C toxins, this result suggests that ABC proteins may be targets of insecticidal three-domain Bt toxins in Coleoptera as well.
DOI: 10.3390/toxins8120362
PubMed: 27929397
PubMed Central: PMC5198556
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Heckel</name><affiliation wicri:level="1"><nlm:affiliation>Department of Entomology, Max Planck Institute for Chemical Ecology, Hans-Knoell-Str. 8, Jena 07745, Germany. heckle@ice.mpg.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Entomology, Max Planck Institute for Chemical Ecology, Hans-Knoell-Str. 8, Jena 07745</wicri:regionArea><wicri:noRegion>07745</wicri:noRegion><wicri:noRegion>07745</wicri:noRegion><wicri:noRegion>Jena 07745</wicri:noRegion></affiliation></author></analytic><series><title level="j">Toxins</title><idno type="eISSN">2072-6651</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ATP Binding Cassette Transporter, Subfamily B (genetics)</term><term>Animals (MeSH)</term><term>Bacterial Proteins (toxicity)</term><term>Cell Line (MeSH)</term><term>Coleoptera (drug effects)</term><term>Coleoptera (genetics)</term><term>Endotoxins (toxicity)</term><term>Female (MeSH)</term><term>Hemolysin Proteins (toxicity)</term><term>Insecticide Resistance (genetics)</term><term>Male (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Coléoptères (effets des médicaments et des substances chimiques)</term><term>Coléoptères (génétique)</term><term>Endotoxines (toxicité)</term><term>Femelle (MeSH)</term><term>Hémolysines (toxicité)</term><term>Lignée cellulaire (MeSH)</term><term>Mâle (MeSH)</term><term>Protéines bactériennes (toxicité)</term><term>Résistance aux insecticides (génétique)</term><term>Sous-famille B de transporteurs à cassette liant l'ATP (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>ATP Binding Cassette Transporter, Subfamily B</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Bacterial Proteins</term><term>Endotoxins</term><term>Hemolysin Proteins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Coleoptera</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Coléoptères</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Coleoptera</term><term>Insecticide Resistance</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Coléoptères</term><term>Résistance aux insecticides</term><term>Sous-famille B de transporteurs à cassette liant l'ATP</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Endotoxines</term><term>Hémolysines</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Female</term><term>Male</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Femelle</term><term>Lignée cellulaire</term><term>Mâle</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><i>Chrysomela tremula</i> is a polyvoltine oligophagous leaf beetle responsible for massive attacks on poplar trees. This beetle is an important model for understanding mechanisms of resistance to <i>Bacillus thuringiensis</i> (Bt) insecticidal toxins, because a resistant <i>C. tremula</i> strain has been found that can survive and reproduce on transgenic poplar trees expressing high levels of the Cry3Aa Bt toxin. Resistance to Cry3Aa in this strain is recessive and is controlled by a single autosomal locus. We used a larval midgut transcriptome for <i>C. tremula</i> to search for candidate resistance genes. We discovered a mutation in an ABC protein, member of the B subfamily homologous to P-glycoprotein, which is genetically linked to Cry3Aa resistance in <i>C. tremula</i>. Cultured insect cells heterologously expressing this ABC protein swell and lyse when incubated with Cry3Aa toxin. In light of previous findings in Lepidoptera implicating A subfamily ABC proteins as receptors for Cry2A toxins and C subfamily proteins as receptors for Cry1A and Cry1C toxins, this result suggests that ABC proteins may be targets of insecticidal three-domain Bt toxins in Coleoptera as well.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27929397</PMID><DateCompleted><Year>2017</Year><Month>10</Month><Day>31</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>02</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2072-6651</ISSN><JournalIssue CitedMedium="Internet"><Volume>8</Volume><Issue>12</Issue><PubDate><Year>2016</Year><Month>12</Month><Day>05</Day></PubDate></JournalIssue><Title>Toxins</Title><ISOAbbreviation>Toxins (Basel)</ISOAbbreviation></Journal><ArticleTitle>A P-Glycoprotein Is Linked to Resistance to the Bacillus thuringiensis Cry3Aa Toxin in a Leaf Beetle.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E362</ELocationID><Abstract><AbstractText><i>Chrysomela tremula</i> is a polyvoltine oligophagous leaf beetle responsible for massive attacks on poplar trees. This beetle is an important model for understanding mechanisms of resistance to <i>Bacillus thuringiensis</i> (Bt) insecticidal toxins, because a resistant <i>C. tremula</i> strain has been found that can survive and reproduce on transgenic poplar trees expressing high levels of the Cry3Aa Bt toxin. Resistance to Cry3Aa in this strain is recessive and is controlled by a single autosomal locus. We used a larval midgut transcriptome for <i>C. tremula</i> to search for candidate resistance genes. We discovered a mutation in an ABC protein, member of the B subfamily homologous to P-glycoprotein, which is genetically linked to Cry3Aa resistance in <i>C. tremula</i>. Cultured insect cells heterologously expressing this ABC protein swell and lyse when incubated with Cry3Aa toxin. In light of previous findings in Lepidoptera implicating A subfamily ABC proteins as receptors for Cry2A toxins and C subfamily proteins as receptors for Cry1A and Cry1C toxins, this result suggests that ABC proteins may be targets of insecticidal three-domain Bt toxins in Coleoptera as well.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pauchet</LastName><ForeName>Yannick</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Entomology, Max Planck Institute for Chemical Ecology, Hans-Knoell-Str. 8, Jena 07745, Germany. ypauchet@ice.mpg.de.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bretschneider</LastName><ForeName>Anne</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Entomology, Max Planck Institute for Chemical Ecology, Hans-Knoell-Str. 8, Jena 07745, Germany. abretschneider@ice.mpg.de.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Augustin</LastName><ForeName>Sylvie</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Unité de Zoologie Forestière, Institut National de la Recherche Agronomique (INRA), 2163 Avenue de la Pomme de Pin, CS 40001 Ardon, Orléans 45075 CEDEX 2, France. sylvie.augustin@inra.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Heckel</LastName><ForeName>David G</ForeName><Initials>DG</Initials><AffiliationInfo><Affiliation>Department of Entomology, Max Planck Institute for Chemical Ecology, Hans-Knoell-Str. 8, Jena 07745, Germany. heckle@ice.mpg.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>12</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Toxins (Basel)</MedlineTA><NlmUniqueID>101530765</NlmUniqueID><ISSNLinking>2072-6651</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018435">ATP Binding Cassette Transporter, Subfamily B</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004731">Endotoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006460">Hemolysin Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C030956">insecticidal crystal protein, Bacillus Thuringiensis</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D018435" MajorTopicYN="N">ATP Binding Cassette Transporter, Subfamily B</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001517" MajorTopicYN="N">Coleoptera</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004731" MajorTopicYN="N">Endotoxins</DescriptorName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006460" MajorTopicYN="N">Hemolysin Proteins</DescriptorName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007305" MajorTopicYN="N">Insecticide Resistance</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">ABC proteins</Keyword><Keyword MajorTopicYN="Y">Bt Cry3Aa toxin</Keyword><Keyword MajorTopicYN="Y">Bt resistance</Keyword><Keyword MajorTopicYN="Y">Chrysomela tremula</Keyword><Keyword MajorTopicYN="Y">leaf beetle</Keyword></KeywordList><CoiStatement>The authors declare no conflicts of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>09</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>11</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>11</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>12</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>12</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>11</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27929397</ArticleId><ArticleId IdType="pii">toxins8120362</ArticleId><ArticleId IdType="doi">10.3390/toxins8120362</ArticleId><ArticleId IdType="pmc">PMC5198556</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Econ Entomol. 2012 Jun;105(3):767-76</Citation><ArticleIdList><ArticleId 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Pauchet</name></noRegion><name sortKey="Bretschneider, Anne" sort="Bretschneider, Anne" uniqKey="Bretschneider A" first="Anne" last="Bretschneider">Anne Bretschneider</name><name sortKey="Heckel, David G" sort="Heckel, David G" uniqKey="Heckel D" first="David G" last="Heckel">David G. Heckel</name></country><country name="France"><region name="Centre-Val de Loire"><name sortKey="Augustin, Sylvie" sort="Augustin, Sylvie" uniqKey="Augustin S" first="Sylvie" last="Augustin">Sylvie Augustin</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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