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...
Main Authors: | , , , , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Elsevier
2023-12-01
|
Series: | Engineering Microbiology |
Subjects: | |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2667370323000152 |
_version_ | 1797400771222831104 |
---|---|
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. |
first_indexed | 2024-03-09T02:00:18Z |
format | Article |
id | doaj.art-0655df9adb7446d59b68645033eeffea |
institution | Directory Open Access Journal |
issn | 2667-3703 |
language | English |
last_indexed | 2024-03-09T02:00:18Z |
publishDate | 2023-12-01 |
publisher | Elsevier |
record_format | Article |
series | Engineering Microbiology |
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 |
work_keys_str_mv | AT kunjiang astrategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT zhechen astrategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT yitingshi astrategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT yuanrongzang astrategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT chengbinshang astrategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT xihuang astrategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT jiahezang astrategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT zhudongbai astrategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT xuyaojiao astrategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT juncai astrategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT xianggao astrategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT kunjiang strategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT zhechen strategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT yitingshi strategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT yuanrongzang strategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT chengbinshang strategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT xihuang strategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT jiahezang strategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT zhudongbai strategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT xuyaojiao strategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT juncai strategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency AT xianggao strategytoenhancetheinsecticidalpotencyofvip3aabyintroducingadditionalcleavagesitestoincreaseitsproteolyticactivationefficiency |