A strategy to enhance the insecticidal potency of Vip3Aa by introducing additional cleavage sites to increase its proteolytic activation efficiency

Microbially derived, protein-based biopesticides have become a vital element in pest management strategies. Vip3 family proteins from Bacillus thuringiensis have distinct characteristics from known insecticidal Cry toxins and show efficient insecticidal activity against several detrimental lepidopte...

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Main Authors: Kun Jiang, Zhe Chen, Yiting Shi, Yuanrong Zang, Chengbin Shang, Xi Huang, Jiahe Zang, Zhudong Bai, Xuyao Jiao, Jun Cai, Xiang Gao
Format: Article
Language:English
Published: Elsevier 2023-12-01
Series:Engineering Microbiology
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2667370323000152
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author Kun Jiang
Zhe Chen
Yiting Shi
Yuanrong Zang
Chengbin Shang
Xi Huang
Jiahe Zang
Zhudong Bai
Xuyao Jiao
Jun Cai
Xiang Gao
author_facet Kun Jiang
Zhe Chen
Yiting Shi
Yuanrong Zang
Chengbin Shang
Xi Huang
Jiahe Zang
Zhudong Bai
Xuyao Jiao
Jun Cai
Xiang Gao
author_sort Kun Jiang
collection DOAJ
description Microbially derived, protein-based biopesticides have become a vital element in pest management strategies. Vip3 family proteins from Bacillus thuringiensis have distinct characteristics from known insecticidal Cry toxins and show efficient insecticidal activity against several detrimental lepidopteran pests. They are considered to be a promising toxic candidate for the management of various detrimental pests. In this study, we found that in addition to the preliminary digestion sites lysine, there are multiple cleavage activation sites in the linker region between domain I (DI) and DII of Vip3Aa. We further demonstrated that by adding more cleavage sites between DI and DII of Vip3Aa, its proteolysis efficiency by midgut proteases can be significantly increased, and correspondingly enhance its insecticidal activity against Spodoptera frugiperda and Helicoverpa armigera larvae. Our study promotes the understanding of the insecticidal mechanism of Vip3 proteins and illustrates an easily implementable strategy to increase the insecticidal potency of Vip3Aa. This facilitates their potential future development and efficient application for sustainable agriculture.
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spelling doaj.art-0655df9adb7446d59b68645033eeffea2023-12-08T04:47:20ZengElsevierEngineering Microbiology2667-37032023-12-0134100083A strategy to enhance the insecticidal potency of Vip3Aa by introducing additional cleavage sites to increase its proteolytic activation efficiencyKun Jiang0Zhe Chen1Yiting Shi2Yuanrong Zang3Chengbin Shang4Xi Huang5Jiahe Zang6Zhudong Bai7Xuyao Jiao8Jun Cai9Xiang Gao10State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China; Corresponding authors.State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, ChinaSchool of Life Sciences, Shandong University, Qingdao 266237, China; Taishan College, Shandong University, Jinan 250100, ChinaState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, ChinaSchool of Life Sciences, Shandong University, Qingdao 266237, ChinaSchool of Life Sciences, Shandong University, Qingdao 266237, ChinaSchool of Life Sciences, Shandong University, Qingdao 266237, ChinaSchool of Life Sciences, Shandong University, Qingdao 266237, ChinaState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, ChinaDepartment of Microbiology, College of Life Sciences, Nankai University, Tianjin 300071, ChinaState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China; Corresponding authors.Microbially derived, protein-based biopesticides have become a vital element in pest management strategies. Vip3 family proteins from Bacillus thuringiensis have distinct characteristics from known insecticidal Cry toxins and show efficient insecticidal activity against several detrimental lepidopteran pests. They are considered to be a promising toxic candidate for the management of various detrimental pests. In this study, we found that in addition to the preliminary digestion sites lysine, there are multiple cleavage activation sites in the linker region between domain I (DI) and DII of Vip3Aa. We further demonstrated that by adding more cleavage sites between DI and DII of Vip3Aa, its proteolysis efficiency by midgut proteases can be significantly increased, and correspondingly enhance its insecticidal activity against Spodoptera frugiperda and Helicoverpa armigera larvae. Our study promotes the understanding of the insecticidal mechanism of Vip3 proteins and illustrates an easily implementable strategy to increase the insecticidal potency of Vip3Aa. This facilitates their potential future development and efficient application for sustainable agriculture.http://www.sciencedirect.com/science/article/pii/S2667370323000152Insecticidal proteinActivation mechanismInsecticidal activity modificationInsecticidal mechanismBacillus thuringiensis
spellingShingle Kun Jiang
Zhe Chen
Yiting Shi
Yuanrong Zang
Chengbin Shang
Xi Huang
Jiahe Zang
Zhudong Bai
Xuyao Jiao
Jun Cai
Xiang Gao
A strategy to enhance the insecticidal potency of Vip3Aa by introducing additional cleavage sites to increase its proteolytic activation efficiency
Engineering Microbiology
Insecticidal protein
Activation mechanism
Insecticidal activity modification
Insecticidal mechanism
Bacillus thuringiensis
title A strategy to enhance the insecticidal potency of Vip3Aa by introducing additional cleavage sites to increase its proteolytic activation efficiency
title_full A strategy to enhance the insecticidal potency of Vip3Aa by introducing additional cleavage sites to increase its proteolytic activation efficiency
title_fullStr A strategy to enhance the insecticidal potency of Vip3Aa by introducing additional cleavage sites to increase its proteolytic activation efficiency
title_full_unstemmed A strategy to enhance the insecticidal potency of Vip3Aa by introducing additional cleavage sites to increase its proteolytic activation efficiency
title_short A strategy to enhance the insecticidal potency of Vip3Aa by introducing additional cleavage sites to increase its proteolytic activation efficiency
title_sort strategy to enhance the insecticidal potency of vip3aa by introducing additional cleavage sites to increase its proteolytic activation efficiency
topic Insecticidal protein
Activation mechanism
Insecticidal activity modification
Insecticidal mechanism
Bacillus thuringiensis
url http://www.sciencedirect.com/science/article/pii/S2667370323000152
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