scholarly journals Prodigiosin Produced by Serratia marcescens Enhances the Insecticidal Activity of Bacillus thuringiensis delta-Endotoxin (Cry1C) against Common Cutworm, Spodoptera litura

1999 ◽  
Vol 24 (4) ◽  
pp. 381-385 ◽  
Author(s):  
Shoji ASANO ◽  
Katsutoshi OGIWARA ◽  
Yoji NAKAGAWA ◽  
Kazushi SUZUKI ◽  
Hidetaka HORI ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Serratia Marcescens ◽  
Insecticidal Activity ◽  
Spodoptera Litura ◽  
Common Cutworm ◽  
Delta Endotoxin

scholarly journals Plasmids and insecticidal activity of delta-endotoxin crystals from Bacillus thuringiensis var. israelensis.

1985 ◽  
Vol 49 (3) ◽  
pp. 573-580 ◽  
Author(s):  
Michio HIMENO ◽  
Masao IKEDA ◽  
Kikuo SEN ◽  
Naoto KOYAMA ◽  
Tohru KOMANO ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Insecticidal Activity ◽  
Delta Endotoxin

Insecticidal Activity and Histopathological Effects of Vip3Aa Protein from Bacillus thuringiensis on Spodoptera litura

2016 ◽  
Vol 26 (10) ◽  
pp. 1774-1780 ◽  
Author(s):  
Feifei Song ◽  
Yunfeng Lin ◽  
Chen Chen ◽  
Ensi Shao ◽  
Xiong Guan ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Insecticidal Activity ◽  
Spodoptera Litura ◽  
Histopathological Effects

scholarly journals Oligomer Formation and Insecticidal Activity of Bacillus thuringiensis Vip3Aa Toxin

Toxins ◽  
2020 ◽  
Vol 12 (4) ◽  
pp. 274 ◽  
Author(s):  
Ensi Shao ◽  
Aishan Zhang ◽  
Yaqi Yan ◽  
Yaomin Wang ◽  
Xinyi Jia ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bacillus Thuringiensis ◽  
Complex Formation ◽  
Insecticidal Activity ◽  
Spodoptera Litura ◽  
Insecticidal Proteins ◽  
Proteolytic Activation ◽  
Oligomer Formation ◽  
Lepidopteran Insects ◽  
Substitution Mutations

Bacillus thuringiensis (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 Spodoptera litura. 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 Spodoptera litura. 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.

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