Search results for "Sf21 cells"

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The Spodoptera exigua ABCC2 Acts as a Cry1A Receptor Independently of its Nucleotide Binding Domain II

2019

ABC proteins are primary-active transporters that require the binding and hydrolysis of ATP to transport substrates across the membrane. Since the first report of an ABCC2 transporter as receptor of Cry1A toxins, the number of ABC transporters known to be involved in the mode of action of Cry toxins has increased. In Spodoptera exigua, a mutation in the SeABCC2 gene is described as genetically linked to resistance to the Bt-product XentariTM. This mutation affects an intracellular domain involved in ATP binding, but not the extracellular loops. We analyzed whether this mutation affects the role of the SeABCC2 as a functional receptor to Cry1A toxins. The results show that Sf21 cells express…

0106 biological sciencesCell SurvivalHealth Toxicology and Mutagenesislcsh:MedicineReceptors Cell SurfaceATP-binding cassette transporterSpodopteraSpodopteraToxicologymedicine.disease_causeBt resistance01 natural sciencesArticleCell LineHemolysin Proteins03 medical and health sciencesBacterial Proteinsmode of actionGTP-Binding ProteinsATP hydrolysismedicineAnimalsReceptor030304 developmental biology0303 health sciencesMutationBacillus thuringiensis ToxinsbiologyChemistryfungilcsh:Rheterologous expressionTransporterbiology.organism_classificationMultidrug Resistance-Associated Protein 2Cell biologyEndotoxins010602 entomologyCyclic nucleotide-binding domainSf21 cellstruncated transporterInsect ProteinsHeterologous expressionMultidrug Resistance-Associated ProteinsToxins
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Purification and reassessment of ligand binding by the recombinant, putative juvenile hormone receptor of the tobacco hornworm, Manduca sexta

1996

The 29 kDa protein from the larval epidermis of the tobacco hornworm, Manduca sexta, that specifically bound photoaffinity analogs of JH I and JH II was produced by a recombinant baculovirus (rJP29). The higher of the two molecular weight forms made corresponded to a protein that could be formed by read‐through of the TGA termination codon to the following TAA. The previously reported, apparent high affinity binding of [methyl‐3H]‐JH I by rJP29 as measured by the dextran‐coated charcoal (DCC) assay [Palli et al., Proc Natl Acad Sci USA 91:6191–6195 (1994)] was found to be artifactual due to endogenous cellular esterases that co‐purified with rJP29 through both DEAE cellulose and MonoQ chrom…

Manduca sextaTn5 cellsjuvenile hormone receptorcellular esterasesSf21 cellsrecombinant baculovirus proteinJH esterasephotoaffinity labelingArchives of Insect Biochemistry and Physiology
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