0000000000037742

AUTHOR

Kanglai He

0000-0001-5959-1042

showing 5 related works from this author

Insecticidal Activity and Synergistic Combinations of Ten Different Bt Toxins against Mythimna separata (Walker)

2018

The oriental armyworm (OAW), Mythimna separata (Walker), is a destructive pest of agricultural crops in Asia and Australia. Commercialized Bt crops have performed very well against their target pests

0301 basic medicineInsecticidesHealth Toxicology and MutagenesisBacterial ToxinsBacillus thuringiensislcsh:MedicineVip3 proteinMothsToxicologymedicine.disease_causeArticleMicrobiology03 medical and health sciencesMythimna separataBacillus thuringiensis<i>Bacillus thuringiensis</i>medicineAnimalsBioassayPotencyCry proteinbiologyToxinlcsh:Rfungifood and beveragesDrug Synergismbiology.organism_classification030104 developmental biologyCry1AcLarvaoriental armywormPEST analysisBacteriaToxins
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Domain shuffling between Vip3Aa and Vip3Ca: chimera stability and insecticidal activity against European, American, African, and Asian pests

2020

The bacterium Bacillus thuringiensis produces insecticidal Vip3 proteins during the vegetative growth phase with activity against several lepidopteran pests. To date, three different Vip3 protein families have been identified based on sequence identity: Vip3A, Vip3B, and Vip3C. In this study, we report the construction of chimeras by exchanging domains between Vip3Aa and Vip3Ca, two proteins with marked specificity differences against lepidopteran pests. We found that some domain combinations made proteins insoluble or prone to degradation by trypsin as most abundant insect gut protease. The soluble and trypsin-stable chimeras, along with the parental proteins Vip3Aa and Vip3Ca, were tested…

InsecticidesAsiaInsectaHealth Toxicology and Mutagenesismedicine.medical_treatmentBacillus thuringiensislcsh:MedicineSpodopteraToxicologyArticleLethal Dose 5003 medical and health sciencesHelicoverpa armigeraBacterial ProteinsProtein DomainsBacillus thuringiensismedicineAnimalsSpodoptera littoralisPest Control Biological030304 developmental biologychemistry.chemical_classification0303 health sciencesProteasebiology030306 microbiologyProtein Stabilitylcsh:RfungiSpodoptera spp.Ostrinia furnacalisSouth Americabiology.organism_classificationFusion proteinAnticarsia gemmatalisAmino acidEuropeAnticarsia gemmatalisspodoptera spp. helicoverpa armigeraBiochemistrychemistryAfricaNorth AmericaMamestra brassicaeOstrinia furnacalis
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The Rapid Evolution of Resistance to Vip3Aa Insecticidal Protein in Mythimna separata (Walker) Is Not Related to Altered Binding to Midgut Receptors

2021

Laboratory selection for resistance of field populations is a well-known and useful tool to understand the potential of insect populations to evolve resistance to insecticides. It provides us with estimates of the frequency of resistance alleles and allows us to study the mechanisms by which insects developed resistance to shed light on the mode of action and optimize resistance management strategies. Here, a field population of Mythimna separata was subjected to laboratory selection with either Vip3Aa, Cry1Ab, or Cry1F insecticidal proteins from Bacillus thuringiensis. The population rapidly evolved resistance to Vip3Aa reaching, after eight generations, a level of &gt;3061-fold resistance…

InsecticidesHealth Toxicology and Mutagenesismedia_common.quotation_subjectPopulationBacillus thuringiensisInsectMothsToxicologyInsecticide Resistance03 medical and health sciencesMythimna separataHemolysin ProteinsBacterial ProteinsBacillus thuringiensis<i>Bacillus thuringiensis</i>cross resistanceBt toxinsAnimalseducationCross-resistance030304 developmental biologymedia_commonGenetics0303 health sciencesLarvaeducation.field_of_studybiologyResistance (ecology)Bacillus thuringiensis Toxins030306 microbiologyCommunicationfungiRMidgutbiology.organism_classificationEndotoxinsLarvaoriental armywormMedicineProtein BindingToxins
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Alteration of a Cry1A Shared Binding Site in a Cry1Ab-Selected Colony of Ostrinia furnacalis

2022

The Asian corn borer, Ostrinia furnacalis (Guenée, 1854), is a highly damaging pest in Asia and the Pacific islands, and larvae feed mainly from corn crops. To determine the suitability of Bt-corn technology for the future control of this pest, understanding the potential to develop resistance to Cry1Ab and the basis of cross-resistance to other Cry1 proteins is of great interest. Here, we have explored the binding of Cry1A proteins to brush border membrane vesicles from two O. furnacalis colonies, one susceptible (ACB-BtS) and one laboratory-selected with Cry1Ab (ACB-AbR). The insects developed resistance to Cry1Ab and showed cross-resistance to Cry1Aa, Cry1Ac, and Cry1F. Binding assays wi…

ChinaBinding SitesBacillus thuringiensis ToxinsCry1 toxinsHealth Toxicology and Mutagenesisfungibinding site modelBacillus thuringiensisRfood and beveragespyramid strategyMothsAsian corn borer; <i>Bacillus thuringiensis</i>; Cry1 toxins; binding site model; pyramid strategyToxicologyAsian corn borerZea maysArticleInsecticide ResistanceLarva<i>Bacillus thuringiensis</i>AnimalsMedicinePest Control BiologicalToxins
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Analysis of cross-resistance to Vip3 proteins in eight insect colonies, from four insect species, selected for resistance to Bacillus thuringiensis i…

2018

Abstract Bacillus thuringiensis Vip3 proteins are synthesized and secreted during the vegetative growth phase. They are activated by gut proteases, recognize and bind to midgut receptors, form pores and lyse cells. We tested the susceptibility to Vip3Aa and Vip3Ca of Cry1A-, Cry2A-, Dipel- and Vip3-resistant insect colonies from different species to determine whether resistance to other insecticidal proteins confers cross-resistance to Vip3 proteins. As expected, the colonies resistant to Cry1A proteins, Dipel (Helicoverpa armigera, Trichoplusia ni, Ostrinia furnacalis and Plodia interpunctella) or Cry2Ab (H. armigera and T. ni) were not cross-resistant to Vip3 proteins. In contrast, H. arm…

0301 basic medicineProteasesInsectabiologymedia_common.quotation_subjectfungi030106 microbiologyBacillus thuringiensisMidgutInsectHelicoverpa armigerabiology.organism_classificationMicrobiologyInsecticide Resistance03 medical and health sciencesBacterial ProteinsBacillus thuringiensisTrichoplusiaAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsCross-resistancemedia_commonOstrinia furnacalisJournal of Invertebrate Pathology
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