Search results for "border membrane-vesicles"

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Lack of Detrimental Effects of Bacillus thuringiensis Cry Toxins on the Insect Predator Chrysoperla carnea : a Toxicological, Histopathological, and …

2006

ABSTRACT The effect of Cry proteins of Bacillus thuringiensis on the green lacewing ( Chrysoperla carnea ) was studied by using a holistic approach which consisted of independent, complementary experimental strategies. Tritrophic experiments were performed, in which lacewing larvae were fed Helicoverpa armigera larvae reared on Cry1Ac, Cry1Ab, or Cry2Ab toxins. In complementary experiments, a predetermined amount of purified Cry1Ac was directly fed to lacewing larvae. In both experiments no effects on prey utilization or fitness parameters were found. Since binding to the midgut is an indispensable step for toxicity of Cry proteins to known target insects, we hypothesized that specific bind…

InsectanoctuidaeBacterial ToxinsBacillus thuringiensisHelicoverpa armigeraApplied Microbiology and BiotechnologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyExiguaInvertebrate MicrobiologyAnimalsBioassaycrystal proteinsPest Control BiologicalChrysoperla carnealarval midgutBacillus thuringiensis ToxinsMicrovilliEcologybiologybinding-sitesfungitoxicityMidgutbiology.organism_classificationspodoptera-exiguaEndotoxinsPRI BioscienceBiochemistryCry1Acmaize expressing cry1abNoctuidaeDigestive Systemborder membrane-vesicleshelicoverpa-armigera lepidopteraFood ScienceBiotechnologyresistant transgenic plants
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The Independent Biological Activity of Bacillus thuringiensis Cry23Aa Protein Against Cylas puncticollis

2020

The Cry23Aa/Cry37Aa proteins from Bacillus thuringiensis (Bt) have been described toxic to Cylas puncticollis larvae. In general, it is believed that Cry23Aa and Cry37Aa act jointly to exert the insecticidal activity, while there is no evidence of their toxicity individually. Therefore, in the present study, the contribution of each protein in the insecticidal activity toward C. puncticollis larvae has been assessed. The results showed that both proteins were toxic for C. puncticollis larvae when tested individually. Contrary to what was claimed previously, our results suggest that the presence of both proteins is not necessary to exert toxicity against C. puncticollis larvae. Also, the bin…

Microbiology (medical)Agriculture and Food SciencesSWEET-POTATO WEEVILlcsh:QR1-502sweet potato weevilsbinary toxinMicrobiologylcsh:Microbiology03 medical and health sciencesmode of actioninsecticidal proteinsBacillus thuringiensisBioassayCry37AaBinding siteSPHAERICUS TOXINMode of action030304 developmental biologybinding assay0303 health sciencesPore-forming toxinLarvabiology030306 microbiologyCRYSTAL PROTEINCOMPONENTSfungiMidgutBiological activityBORDER MEMBRANE-VESICLESENTOMOPATHOGENIC FUNGIbiology.organism_classificationEFFICACYBiochemistrybioassayCOLEOPTERABRUNNEUSRESISTANCEFrontiers in Microbiology
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