6533b86efe1ef96bd12ccadb
RESEARCH PRODUCT
Interaction of Bacillus thuringiensis Cry1 and Vip3A Proteins with Spodoptera frugiperda Midgut Binding Sites
Janete A D SenaCarmen Sara Hernández-rodríguezJuan Ferrésubject
Bioquímicaanimal structuresBiotecnologia agrícolaBacillus thuringiensisPlasma protein bindingSpodopteraSpodopteraHemolysin ProteinsApplied Microbiology and BiotechnologyProtein–protein interactionMicrobiologyLethal Dose 50Hemolysin ProteinsBacterial ProteinsBacillus thuringiensisPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteBacillus thuringiensis ToxinsEcologybiologyfungifood and beveragesMidgutbiology.organism_classificationBacillalesEndotoxinsGastrointestinal TractBiochemistryLarvasense organsProteïnesProtein BindingFood ScienceBiotechnologydescription
ABSTRACT Vip3Aa, Vip3Af, Cry1Ab, and Cry1Fa were tested for their toxicities and binding interactions. Vip3A proteins were more toxic than Cry1 proteins. Binding assays showed independent specific binding sites for Cry1 and Vip3A proteins. Cry1Ab and Cry1Fa competed for the same binding sites, whereas Vip3Aa competed for those of Vip3Af.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2009-01-01 | Applied and Environmental Microbiology |