Oligomer Formation and Insecticidal Activity of <i>Bacillus thuringiensis</i> Vip3Aa Toxin
<i>Bacillus thuringiensis</i> (Bt) Vip3A proteins are important insecticidal proteins used for control of lepidopteran insects. However, the mode of action of Vip3A toxin is still unclear. In this study, the amino acid residue S164 in Vip3Aa was identified to be critical for the toxicity...
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MDPI AG
2020-04-01
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| Series: | Toxins |
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| Online Access: | https://www.mdpi.com/2072-6651/12/4/274 |
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| author | Ensi Shao Aishan Zhang Yaqi Yan Yaomin Wang Xinyi Jia Li Sha Xiong Guan Ping Wang Zhipeng Huang |
| author_facet | Ensi Shao Aishan Zhang Yaqi Yan Yaomin Wang Xinyi Jia Li Sha Xiong Guan Ping Wang Zhipeng Huang |
| author_sort | Ensi Shao |
| collection | DOAJ |
| description | <i>Bacillus thuringiensis</i> (Bt) Vip3A proteins are important insecticidal proteins used for control of lepidopteran insects. However, the mode of action of Vip3A toxin is still unclear. In this study, the amino acid residue S164 in Vip3Aa was identified to be critical for the toxicity in <i>Spodoptera litura</i>. Results from substitution mutations of the S164 indicate that the insecticidal activity of Vip3Aa correlated with the formation of a >240 kDa complex of the toxin upon proteolytic activation. The >240 kDa complex was found to be composed of the 19 kDa and the 65 kDa fragments of Vip3Aa. Substitution of the S164 in Vip3Aa protein with Ala or Pro resulted in loss of the >240 kDa complex and loss of toxicity in <i>Spodoptera litura</i>. In contrast, substitution of S164 with Thr did not affect the >240 kDa complex formation, and the toxicity of the mutant was only reduced by 35%. Therefore, the results from this study indicated that formation of the >240 kDa complex correlates with the toxicity of Vip3Aa in insects and the residue S164 is important for the formation of the complex. |
| first_indexed | 2024-03-10T20:16:13Z |
| format | Article |
| id | doaj.art-3dc6e60259dc4f9e92539b6590217966 |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-03-10T20:16:13Z |
| publishDate | 2020-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-3dc6e60259dc4f9e92539b65902179662023-11-19T22:30:27ZengMDPI AGToxins2072-66512020-04-0112427410.3390/toxins12040274Oligomer Formation and Insecticidal Activity of <i>Bacillus thuringiensis</i> Vip3Aa ToxinEnsi Shao0Aishan Zhang1Yaqi Yan2Yaomin Wang3Xinyi Jia4Li Sha5Xiong Guan6Ping Wang7Zhipeng Huang8China National Engineering Research Center of JUNCAO Technology, College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, Fujian, ChinaChina National Engineering Research Center of JUNCAO Technology, College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, Fujian, ChinaChina National Engineering Research Center of JUNCAO Technology, College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, Fujian, ChinaChina National Engineering Research Center of JUNCAO Technology, College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, Fujian, ChinaChina National Engineering Research Center of JUNCAO Technology, College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, Fujian, ChinaChina National Engineering Research Center of JUNCAO Technology, College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, Fujian, ChinaKey Laboratory of Biopesticide and Chemical Biology (Ministry of Education), College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou 350002, Fujian, ChinaDepartment of Entomology, Cornell University, Geneva, NY 14456, USAChina National Engineering Research Center of JUNCAO Technology, College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, Fujian, China<i>Bacillus thuringiensis</i> (Bt) Vip3A proteins are important insecticidal proteins used for control of lepidopteran insects. However, the mode of action of Vip3A toxin is still unclear. In this study, the amino acid residue S164 in Vip3Aa was identified to be critical for the toxicity in <i>Spodoptera litura</i>. Results from substitution mutations of the S164 indicate that the insecticidal activity of Vip3Aa correlated with the formation of a >240 kDa complex of the toxin upon proteolytic activation. The >240 kDa complex was found to be composed of the 19 kDa and the 65 kDa fragments of Vip3Aa. Substitution of the S164 in Vip3Aa protein with Ala or Pro resulted in loss of the >240 kDa complex and loss of toxicity in <i>Spodoptera litura</i>. In contrast, substitution of S164 with Thr did not affect the >240 kDa complex formation, and the toxicity of the mutant was only reduced by 35%. Therefore, the results from this study indicated that formation of the >240 kDa complex correlates with the toxicity of Vip3Aa in insects and the residue S164 is important for the formation of the complex.https://www.mdpi.com/2072-6651/12/4/274<i>Bacillus thuringiensis</i>Vip3A<i>Spodoptera litura</i>site-directed mutagenesis |
| spellingShingle | Ensi Shao Aishan Zhang Yaqi Yan Yaomin Wang Xinyi Jia Li Sha Xiong Guan Ping Wang Zhipeng Huang Oligomer Formation and Insecticidal Activity of <i>Bacillus thuringiensis</i> Vip3Aa Toxin Toxins <i>Bacillus thuringiensis</i> Vip3A <i>Spodoptera litura</i> site-directed mutagenesis |
| title | Oligomer Formation and Insecticidal Activity of <i>Bacillus thuringiensis</i> Vip3Aa Toxin |
| title_full | Oligomer Formation and Insecticidal Activity of <i>Bacillus thuringiensis</i> Vip3Aa Toxin |
| title_fullStr | Oligomer Formation and Insecticidal Activity of <i>Bacillus thuringiensis</i> Vip3Aa Toxin |
| title_full_unstemmed | Oligomer Formation and Insecticidal Activity of <i>Bacillus thuringiensis</i> Vip3Aa Toxin |
| title_short | Oligomer Formation and Insecticidal Activity of <i>Bacillus thuringiensis</i> Vip3Aa Toxin |
| title_sort | oligomer formation and insecticidal activity of i bacillus thuringiensis i vip3aa toxin |
| topic | <i>Bacillus thuringiensis</i> Vip3A <i>Spodoptera litura</i> site-directed mutagenesis |
| url | https://www.mdpi.com/2072-6651/12/4/274 |
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