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    <titleInfo>
      <title>Toxin stability improvement and toxicity increase against dipteran and lepidopteran larvae of Bacillus thuringiensis crystal protein Cry2Aa</title>
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      <namePart type="family">Elleuch</namePart>
      <namePart type="given">J.</namePart>
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      <namePart type="family">Jaoua</namePart>
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      <affiliation>IRD</affiliation>
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    <name type="personnal">
      <namePart type="family">Ginibre</namePart>
      <namePart type="given">Carole</namePart>
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        <roleTerm type="text">auteur</roleTerm>
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    <name type="personnal">
      <namePart type="family">Chandre</namePart>
      <namePart type="given">Fabrice</namePart>
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      <namePart type="family">Tounsi</namePart>
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        <roleTerm type="text">auteur</roleTerm>
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    <name type="personnal">
      <namePart type="family">Zghal</namePart>
      <namePart type="given">R. Z.</namePart>
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    <genre authority="local">journalArticle</genre>
    <language>
      <languageTerm type="code" authority="iso639-2b">eng</languageTerm>
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    <abstract>BACKGROUNDBacillus thuringiensis -endotoxins are the most widely used biopesticides for controlling economically important crop pests and disease vectors. Improving their efficacy is of great benefit. Here, an improvement in Cry2Aa-endotoxin toxicity was attempted via a cry gene over expression system using P20 from B. thuringiensis israelensis. RESULTSThe coexpression of Cry2Aa with P20 resulted in a seven fold increase in its production yield in B. thuringiensis. Generated crystals proved to be significantly more toxic (505.207 mu gg(-1), 1.99mgL(-1) and 1.49mgL(-1)) than the P20-lacking control (720.78 mu gg(-1), 705.69mgL(-1) and 508.51mgL(-1)) against Ephestia kuehniella, Aedes aegypti and Culex pipiens larvae respectively. In vitro, processing experiments revealed a P20-mediated protection of Cry2Aa against degradation under larval gut conditions. Thus, P20 could promote the maintenance of a tightly packaged conformation of Cry2Aa toxins in the larval midgut upon correct activation and binding to its membrane receptors. CONCLUSIONBased on their resistance against excessive proteolysis, Cry2Aa-endotoxins, produced in the presence of P20, could be considered as a successful control agent for E. kuehniella and an effective alternative for mosquito control, implying its possible exploitation in pest management programmes.</abstract>
    <targetAudience authority="marctarget">specialized</targetAudience>
    <subject>
      <topic>P20 helper protein</topic>
      <topic>Cry2Aa toxin</topic>
      <topic>larvicidal activity improvement</topic>
      <topic>protection against excessive proteolysis</topic>
    </subject>
    <classification authority="local">052</classification>
    <classification authority="local">076</classification>
    <classification authority="local">020</classification>
    <classification authority="local">084</classification>
    <relatedItem type="host">
      <titleInfo>
        <title>Pest Management Science</title>
      </titleInfo>
      <part>
        <detail type="volume">
          <number>72</number>
        </detail>
        <detail type="volume">
          <number>12</number>
        </detail>
        <extent unit="pages">
          <list> 2240-2246</list>
        </extent>
      </part>
      <originInfo>
        <dateIssued>2016</dateIssued>
      </originInfo>
      <identifier type="issn">1526-498X</identifier>
    </relatedItem>
    <identifier type="uri">https://www.documentation.ird.fr/hor/fdi:010068318</identifier>
    <identifier type="doi">10.1002/ps.4261</identifier>
    <identifier type="issn">1526-498X</identifier>
    <location>
      <shelfLocator>[F B010068318]</shelfLocator>
      <url usage="primary display" access="object in context">https://www.documentation.ird.fr/hor/fdi:010068318</url>
      <url access="row object">https://www.documentation.ird.fr/intranet/publi/2016/11/010068318.pdf</url>
    </location>
    <accessCondition type="restriction access" displayLabel="Accès réservé">Accès réservé (Intranet de l'IRD)</accessCondition>
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      <recordContentSource>IRD - Base Horizon / Pleins textes</recordContentSource>
      <recordCreationDate encoding="w3cdtf">2016-12-06</recordCreationDate>
      <recordChangeDate encoding="w3cdtf">2017-08-23</recordChangeDate>
      <recordIdentifier>fdi:010068318</recordIdentifier>
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        <languageTerm authority="iso639-2b">fre</languageTerm>
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