Insect Hsp90 Chaperone Assists <named-content content-type="genus-species">Bacillus thuringiensis</named-content> Cry Toxicity by Enhancing Protoxin Binding to the Receptor and by Protecting Protoxin from Gut Protease Degradation

Insect Hsp90 Chaperone Assists <named-content content-type="genus-species">Bacillus thuringiensis</named-content> Cry Toxicity by Enhancing Protoxin Binding to the Receptor and by Protecting Protoxin from Gut Protease Degradation

ABSTRACT Bacillus thuringiensis Cry proteins are pore-forming insecticidal toxins with specificity against different crop pests and insect vectors of human diseases. Previous work suggested that the insect host Hsp90 chaperone could be involved in Cry toxin action. Here, we show that the interaction...

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Autores principales: Blanca I. García-Gómez, Sayra N. Cano, Erika E. Zagal, Edgar Dantán-Gonzalez, Alejandra Bravo, Mario Soberón
Formato: article
Lenguaje:EN
Publicado: American Society for Microbiology 2019
Materias:
Bacillus thuringiensis
Cry toxins
receptor binding
protein chaperone
protoxins
Microbiology
QR1-502
Acceso en línea:https://doaj.org/article/a1fe8557564b4bcf89e9d16eff3ef332
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