V-ATPase C Acts as a Receptor for Bacillus thuringiensis Cry2Ab and Enhances Cry2Ab Toxicity to Helicoverpa armigera

Pin Li; Yuge Zhao; Ningbo Zhang; Xue Yao; Xianchun Li; Mengfang Du; Jizhen Wei; Shiheng An

doi:10.3390/insects15110895

V-ATPase C Acts as a Receptor for Bacillus thuringiensis Cry2Ab and Enhances Cry2Ab Toxicity to Helicoverpa armigera

Pin Li, Yuge Zhao, Ningbo Zhang, Xue Yao, Xianchun Li, Mengfang Du, Jizhen Wei, Shiheng An

Research output: Contribution to journal › Article › peer-review

Abstract

Currently, identified receptors do not fully elucidate the mechanism of action for Cry2Ab. Here, the results showed that Cry2Ab decreased HaV-ATPase C expression, and there was a confirmed interaction between them. The knockdown of HaV-ATPase C reduces Cry2Ab cytotoxicity, while its overexpression enhances it. Additionally, enhanced effects against H. armigera result from the combination of Cry2Ab and V-ATPase C. These findings demonstrate that V-ATPase C acts as a functional receptor for Cry2Ab in Helicoverpa armigera, and the synergistic interaction between them offers a promising strategy to enhance Cry2Ab toxicity.

Original language	English (US)
Article number	895
Journal	Insects
Volume	15
Issue number	11
DOIs	https://doi.org/10.3390/insects15110895
State	Published - Nov 2024

Keywords

Bacillus thuringiensis
binding
Cry2Ab
Helicoverpa armigera
toxicity
V-ATPase C

ASJC Scopus subject areas

Insect Science

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10.3390/insects15110895

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title = "V-ATPase C Acts as a Receptor for Bacillus thuringiensis Cry2Ab and Enhances Cry2Ab Toxicity to Helicoverpa armigera",

abstract = "Currently, identified receptors do not fully elucidate the mechanism of action for Cry2Ab. Here, the results showed that Cry2Ab decreased HaV-ATPase C expression, and there was a confirmed interaction between them. The knockdown of HaV-ATPase C reduces Cry2Ab cytotoxicity, while its overexpression enhances it. Additionally, enhanced effects against H. armigera result from the combination of Cry2Ab and V-ATPase C. These findings demonstrate that V-ATPase C acts as a functional receptor for Cry2Ab in Helicoverpa armigera, and the synergistic interaction between them offers a promising strategy to enhance Cry2Ab toxicity.",

keywords = "Bacillus thuringiensis, binding, Cry2Ab, Helicoverpa armigera, toxicity, V-ATPase C",

author = "Pin Li and Yuge Zhao and Ningbo Zhang and Xue Yao and Xianchun Li and Mengfang Du and Jizhen Wei and Shiheng An",

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doi = "10.3390/insects15110895",

language = "English (US)",

volume = "15",

journal = "Insects",

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T1 - V-ATPase C Acts as a Receptor for Bacillus thuringiensis Cry2Ab and Enhances Cry2Ab Toxicity to Helicoverpa armigera

AU - Li, Pin

AU - Zhao, Yuge

AU - Zhang, Ningbo

AU - Yao, Xue

AU - Li, Xianchun

AU - Du, Mengfang

AU - Wei, Jizhen

AU - An, Shiheng

PY - 2024/11

Y1 - 2024/11

N2 - Currently, identified receptors do not fully elucidate the mechanism of action for Cry2Ab. Here, the results showed that Cry2Ab decreased HaV-ATPase C expression, and there was a confirmed interaction between them. The knockdown of HaV-ATPase C reduces Cry2Ab cytotoxicity, while its overexpression enhances it. Additionally, enhanced effects against H. armigera result from the combination of Cry2Ab and V-ATPase C. These findings demonstrate that V-ATPase C acts as a functional receptor for Cry2Ab in Helicoverpa armigera, and the synergistic interaction between them offers a promising strategy to enhance Cry2Ab toxicity.

AB - Currently, identified receptors do not fully elucidate the mechanism of action for Cry2Ab. Here, the results showed that Cry2Ab decreased HaV-ATPase C expression, and there was a confirmed interaction between them. The knockdown of HaV-ATPase C reduces Cry2Ab cytotoxicity, while its overexpression enhances it. Additionally, enhanced effects against H. armigera result from the combination of Cry2Ab and V-ATPase C. These findings demonstrate that V-ATPase C acts as a functional receptor for Cry2Ab in Helicoverpa armigera, and the synergistic interaction between them offers a promising strategy to enhance Cry2Ab toxicity.

KW - Bacillus thuringiensis

KW - binding

KW - Cry2Ab

KW - Helicoverpa armigera

KW - toxicity

KW - V-ATPase C

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V-ATPase C Acts as a Receptor for Bacillus thuringiensis Cry2Ab and Enhances Cry2Ab Toxicity to Helicoverpa armigera

Abstract

Keywords

ASJC Scopus subject areas

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