Histopathological and combinatorial effects of the metalloprotease InhA1 and Cry proteins of Bacillus thuringiensis against Spodoptera littoralis.
Identifieur interne : 001631 ( Main/Exploration ); précédent : 001630; suivant : 001632Histopathological and combinatorial effects of the metalloprotease InhA1 and Cry proteins of Bacillus thuringiensis against Spodoptera littoralis.
Auteurs : Ines Dammak [Tunisie] ; Mariam Dammak [Tunisie] ; Slim Tounsi [Tunisie]Source :
- International journal of biological macromolecules [ 1879-0003 ] ; 2015.
Descripteurs français
- KwdFr :
- Analyse de séquence d'ADN (MeSH), Animaux (MeSH), Antibiose (MeSH), Bacillus thuringiensis (physiologie), Clonage moléculaire (MeSH), Escherichia coli (génétique), Escherichia coli (métabolisme), Expression des gènes (MeSH), Insecticides (pharmacologie), Larve (effets des médicaments et des substances chimiques), Metalloendopeptidases (génétique), Metalloendopeptidases (métabolisme), Metalloendopeptidases (pharmacologie), Spodoptera (physiologie), Toxines bactériennes (génétique), Toxines bactériennes (métabolisme), Toxines bactériennes (pharmacologie).
- MESH :
- effets des médicaments et des substances chimiques : Larve.
- génétique : Escherichia coli, Metalloendopeptidases, Toxines bactériennes.
- métabolisme : Escherichia coli, Metalloendopeptidases, Toxines bactériennes.
- pharmacologie : Insecticides, Metalloendopeptidases, Toxines bactériennes.
- physiologie : Bacillus thuringiensis, Spodoptera.
- Analyse de séquence d'ADN, Animaux, Antibiose, Clonage moléculaire, Expression des gènes.
English descriptors
- KwdEn :
- Animals (MeSH), Antibiosis (MeSH), Bacillus thuringiensis (physiology), Bacterial Toxins (genetics), Bacterial Toxins (metabolism), Bacterial Toxins (pharmacology), Cloning, Molecular (MeSH), Escherichia coli (genetics), Escherichia coli (metabolism), Gene Expression (MeSH), Insecticides (pharmacology), Larva (drug effects), Metalloendopeptidases (genetics), Metalloendopeptidases (metabolism), Metalloendopeptidases (pharmacology), Sequence Analysis, DNA (MeSH), Spodoptera (physiology).
- MESH :
- chemical , genetics : Bacterial Toxins, Metalloendopeptidases.
- chemical , metabolism : Bacterial Toxins, Metalloendopeptidases.
- chemical , pharmacology : Bacterial Toxins, Insecticides, Metalloendopeptidases.
- drug effects : Larva.
- genetics : Escherichia coli.
- metabolism : Escherichia coli.
- physiology : Bacillus thuringiensis, Spodoptera.
- Animals, Antibiosis, Cloning, Molecular, Gene Expression, Sequence Analysis, DNA.
Abstract
The zinc metalloprotease (InhA) of Bacillus thuringiensis specifically hydrolyzes cecropins and attacins, two antibacterial peptides in the immune hemolymph of insects, leading to a high resistance of the bacteria to the humoral defense system of its host. In the present study, the inhA gene of B. thuringiensis strain BUPM28 was cloned and the nucleotide sequence analysis revealed that it was identical to that of B. thuringiensis 8010. The expressed InhA1 protein in Escherichia coli showed toxicity to neonate Spodoptera littoralis larvae with a LC50 of 2.07±0.72μg/cm(2). Study of the effect of combining Cry proteins with InhA1 showed that one improves the toxicity of the other one against S. littoralis. Investigation of the histopathological effect of this metalloprotease showed an extensive damage of S. littoralis epithelium tissue. These results provide an insight to the use of InhA as supplement to Cry toxins to improve the efficacy of B. thuringiensis formulations and to overcome possible resistance problems.
DOI: 10.1016/j.ijbiomac.2015.09.006
PubMed: 26358555
Affiliations:
Links toward previous steps (curation, corpus...)
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In the present study, the inhA gene of B. thuringiensis strain BUPM28 was cloned and the nucleotide sequence analysis revealed that it was identical to that of B. thuringiensis 8010. The expressed InhA1 protein in Escherichia coli showed toxicity to neonate Spodoptera littoralis larvae with a LC50 of 2.07±0.72μg/cm(2). Study of the effect of combining Cry proteins with InhA1 showed that one improves the toxicity of the other one against S. littoralis. Investigation of the histopathological effect of this metalloprotease showed an extensive damage of S. littoralis epithelium tissue. These results provide an insight to the use of InhA as supplement to Cry toxins to improve the efficacy of B. thuringiensis formulations and to overcome possible resistance problems. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26358555</PMID><DateCompleted><Year>2016</Year><Month>10</Month><Day>13</Day></DateCompleted><DateRevised><Year>2016</Year><Month>12</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0003</ISSN><JournalIssue CitedMedium="Internet"><Volume>81</Volume><PubDate><Year>2015</Year><Month>Nov</Month></PubDate></JournalIssue><Title>International journal of biological macromolecules</Title><ISOAbbreviation>Int J Biol Macromol</ISOAbbreviation></Journal><ArticleTitle>Histopathological and combinatorial effects of the metalloprotease InhA1 and Cry proteins of Bacillus thuringiensis against Spodoptera littoralis.</ArticleTitle><Pagination><MedlinePgn>759-62</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijbiomac.2015.09.006</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0141-8130(15)00621-2</ELocationID><Abstract><AbstractText>The zinc metalloprotease (InhA) of Bacillus thuringiensis specifically hydrolyzes cecropins and attacins, two antibacterial peptides in the immune hemolymph of insects, leading to a high resistance of the bacteria to the humoral defense system of its host. In the present study, the inhA gene of B. thuringiensis strain BUPM28 was cloned and the nucleotide sequence analysis revealed that it was identical to that of B. thuringiensis 8010. The expressed InhA1 protein in Escherichia coli showed toxicity to neonate Spodoptera littoralis larvae with a LC50 of 2.07±0.72μg/cm(2). Study of the effect of combining Cry proteins with InhA1 showed that one improves the toxicity of the other one against S. littoralis. Investigation of the histopathological effect of this metalloprotease showed an extensive damage of S. littoralis epithelium tissue. These results provide an insight to the use of InhA as supplement to Cry toxins to improve the efficacy of B. thuringiensis formulations and to overcome possible resistance problems. </AbstractText><CopyrightInformation>Copyright © 2015 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dammak</LastName><ForeName>Ines</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Laboratory of Biopesticides, Centre of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, 3018 Sfax, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dammak</LastName><ForeName>Mariam</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory of Biopesticides, Centre of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, 3018 Sfax, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tounsi</LastName><ForeName>Slim</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Laboratory of Biopesticides, Centre of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, 3018 Sfax, Tunisia. Electronic address: slim.tounsi@cbs.rnrt.tn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>09</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Int J Biol Macromol</MedlineTA><NlmUniqueID>7909578</NlmUniqueID><ISSNLinking>0141-8130</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001427">Bacterial Toxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007306">Insecticides</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.-</RegistryNumber><NameOfSubstance UI="D008666">Metalloendopeptidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000898" MajorTopicYN="Y">Antibiosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001413" MajorTopicYN="N">Bacillus thuringiensis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001427" MajorTopicYN="N">Bacterial Toxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007306" MajorTopicYN="N">Insecticides</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007814" MajorTopicYN="N">Larva</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008666" MajorTopicYN="N">Metalloendopeptidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017422" MajorTopicYN="N">Sequence Analysis, DNA</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018411" MajorTopicYN="N">Spodoptera</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">B. thuringiensis</Keyword><Keyword MajorTopicYN="N">InhA1</Keyword><Keyword MajorTopicYN="N">Metalloprotease</Keyword><Keyword MajorTopicYN="N">S. littoralis</Keyword><Keyword MajorTopicYN="N">Toxicity</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>06</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>08</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>09</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>9</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>9</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>10</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26358555</ArticleId><ArticleId IdType="pii">S0141-8130(15)00621-2</ArticleId><ArticleId IdType="doi">10.1016/j.ijbiomac.2015.09.006</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Tunisie</li></country></list><tree><country name="Tunisie"><noRegion><name sortKey="Dammak, Ines" sort="Dammak, Ines" uniqKey="Dammak I" first="Ines" last="Dammak">Ines Dammak</name></noRegion><name sortKey="Dammak, Mariam" sort="Dammak, Mariam" uniqKey="Dammak M" first="Mariam" last="Dammak">Mariam Dammak</name><name sortKey="Tounsi, Slim" sort="Tounsi, Slim" uniqKey="Tounsi S" first="Slim" last="Tounsi">Slim Tounsi</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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