Specific Epitopes of Domains II and III of Bacillus thuringiensis Cry1Ab Toxin Involved in the Sequential Interaction with Cadherin and Aminopeptidase-N Receptors in Manduca sexta

The Bacillus thuringiensis Cry toxins are specific to different insects. In Manduca sexta cadherin (Bt-R1) and aminopeptidase-N (APN) proteins are recognized as Cry1A receptors. Previous work showed that Cry1Ab binds to Bt-R1 promoting the formation of a pre-pore oligomer that binds to APN leading t...

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Veröffentlicht in:	The Journal of biological chemistry 2006-11, Vol.281 (45), p.34032-34039
Hauptverfasser:	Gómez, Isabel, Arenas, Iván, Benitez, Itzel, Miranda-Ríos, Juan, Becerril, Baltazar, Grande, Ricardo, Almagro, Juan Carlos, Bravo, Alejandra, Soberón, Mario
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Bacillus thuringiensis Bacillus thuringiensis - chemistry Bacillus thuringiensis Toxins Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacterial Proteins - toxicity Bacterial Toxins - chemistry Bacterial Toxins - metabolism Bacterial Toxins - toxicity Cadherins - metabolism CD13 Antigens - metabolism Endotoxins - chemistry Endotoxins - metabolism Endotoxins - toxicity Epitopes - analysis Epitopes - chemistry Hemolysin Proteins - chemistry Hemolysin Proteins - metabolism Hemolysin Proteins - toxicity Immunization Immunoglobulin Variable Region - immunology Immunoglobulin Variable Region - metabolism Insecticides - chemistry Insecticides - metabolism Insecticides - toxicity Manduca - metabolism Manduca sexta Microvilli - metabolism Peptide Library Peptides - chemistry Peptides - immunology Peptides - metabolism Pest Control, Biological Protein Binding Rabbits Receptors, Cell Surface - metabolism Recombinant Proteins - chemistry Recombinant Proteins - metabolism
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