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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spelling	oai:doaj.org-article:a1fe8557564b4bcf89e9d16eff3ef3322021-11-15T15:54:46ZInsect 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 Degradation10.1128/mBio.02775-192150-7511https://doaj.org/article/a1fe8557564b4bcf89e9d16eff3ef3322019-12-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.02775-19https://doaj.org/toc/2150-7511ABSTRACT 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 of Cry toxins with insect Hsp90 constitutes a positive loop to enhance the performance of these toxins. Plutella xylostella Hsp90 (PxHsp90) greatly enhanced Cry1Ab or Cry1Ac toxicity when fed together to P. xylostella larvae and also in the less susceptible Spodoptera frugiperda larvae. PxHsp90 bound Cry1Ab and Cry1Ac protoxins in an ATP- and chaperone activity-dependent interaction. The chaperone Hsp90 participates in the correct folding of proteins and may suppress mutations of some client proteins, and we show here that PxHsp90 recovered the toxicity of the Cry1AbG439D protoxin affected in receptor binding, in contrast to the Cry1AbR99E or Cry1AbE129K mutant, affected in oligomerization or membrane insertion, respectively, which showed a slight toxicity improvement. Specifically, PxHsp90 enhanced the binding of Cry1AbG439D protoxin to the cadherin receptor. Furthermore, PxHsp90 protected Cry1A protoxins from degradation by insect midgut proteases. Our data show that PxHsp90 assists Cry1A proteins by enhancing their binding to the receptor and by protecting Cry protoxin from gut protease degradation. Finally, we show that the insect cochaperone protein PxHsp70 also increases the toxicity of Cry1Ac in P. xylostella larvae, in contrast to a bacterial GroEL chaperone, which had a marginal effect, indicating that the use of insect chaperones along with Cry toxins could have important biotechnological applications for the improvement of Cry insecticidal activity, resulting in effective control of insect pests. IMPORTANCE Bacillus thuringiensis took advantage of important insect cellular proteins, such as chaperones, involved in maintaining protein homeostasis, to enhance its insecticidal activity. This constitutes a positive loop where the concentrations of Hsp90 and Hsp70 in the gut lumen are likely to increase as midgut cells burst due to Cry1A pore formation action. Hsp90 protects Cry1A protoxin from degradation and enhances receptor binding, resulting in increased toxicity. The effect of insect chaperones on Cry toxicity could have important biotechnological applications to enhance the toxicity of Cry proteins to insect pests, especially those that show low susceptibility to these toxins.Blanca I. García-GómezSayra N. CanoErika E. ZagalEdgar Dantán-GonzalezAlejandra BravoMario SoberónAmerican Society for MicrobiologyarticleBacillus thuringiensisCry toxinsreceptor bindingprotein chaperoneprotoxinsMicrobiologyQR1-502ENmBio, Vol 10, Iss 6 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Bacillus thuringiensis Cry toxins receptor binding protein chaperone protoxins Microbiology QR1-502
spellingShingle	Bacillus thuringiensis Cry toxins receptor binding protein chaperone protoxins Microbiology QR1-502 Blanca I. García-Gómez Sayra N. Cano Erika E. Zagal Edgar Dantán-Gonzalez Alejandra Bravo Mario Soberón 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
description	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 of Cry toxins with insect Hsp90 constitutes a positive loop to enhance the performance of these toxins. Plutella xylostella Hsp90 (PxHsp90) greatly enhanced Cry1Ab or Cry1Ac toxicity when fed together to P. xylostella larvae and also in the less susceptible Spodoptera frugiperda larvae. PxHsp90 bound Cry1Ab and Cry1Ac protoxins in an ATP- and chaperone activity-dependent interaction. The chaperone Hsp90 participates in the correct folding of proteins and may suppress mutations of some client proteins, and we show here that PxHsp90 recovered the toxicity of the Cry1AbG439D protoxin affected in receptor binding, in contrast to the Cry1AbR99E or Cry1AbE129K mutant, affected in oligomerization or membrane insertion, respectively, which showed a slight toxicity improvement. Specifically, PxHsp90 enhanced the binding of Cry1AbG439D protoxin to the cadherin receptor. Furthermore, PxHsp90 protected Cry1A protoxins from degradation by insect midgut proteases. Our data show that PxHsp90 assists Cry1A proteins by enhancing their binding to the receptor and by protecting Cry protoxin from gut protease degradation. Finally, we show that the insect cochaperone protein PxHsp70 also increases the toxicity of Cry1Ac in P. xylostella larvae, in contrast to a bacterial GroEL chaperone, which had a marginal effect, indicating that the use of insect chaperones along with Cry toxins could have important biotechnological applications for the improvement of Cry insecticidal activity, resulting in effective control of insect pests. IMPORTANCE Bacillus thuringiensis took advantage of important insect cellular proteins, such as chaperones, involved in maintaining protein homeostasis, to enhance its insecticidal activity. This constitutes a positive loop where the concentrations of Hsp90 and Hsp70 in the gut lumen are likely to increase as midgut cells burst due to Cry1A pore formation action. Hsp90 protects Cry1A protoxin from degradation and enhances receptor binding, resulting in increased toxicity. The effect of insect chaperones on Cry toxicity could have important biotechnological applications to enhance the toxicity of Cry proteins to insect pests, especially those that show low susceptibility to these toxins.
format	article
author	Blanca I. García-Gómez Sayra N. Cano Erika E. Zagal Edgar Dantán-Gonzalez Alejandra Bravo Mario Soberón
author_facet	Blanca I. García-Gómez Sayra N. Cano Erika E. Zagal Edgar Dantán-Gonzalez Alejandra Bravo Mario Soberón
author_sort	Blanca I. García-Gómez
title	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
title_short	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
title_full	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
title_fullStr	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
title_full_unstemmed	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
title_sort	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
publisher	American Society for Microbiology
publishDate	2019
url	https://doaj.org/article/a1fe8557564b4bcf89e9d16eff3ef332
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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

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