Vip3A is responsible for the potency of <i>Bacillus thuringiensis</i> 9816C culture supernatant against Helicoverpa armigera and Spodoptera exigua. Cai, J., Xiao, L., Yan, B., Bin, G., Chen, Y., & Ren, G. The Journal of General and Applied Microbiology, 52(2):83-89, 4, 2006.
Vip3A is responsible for the potency of <i>Bacillus thuringiensis</i> 9816C culture supernatant against Helicoverpa armigera and Spodoptera exigua. [pdf]Paper  abstract   bibtex   
Culture supernatant of Bacillus thuringiensis 9816C had high toxicity against Helicoverpa armigera and Spodoptera exigua. However, it lost insecticidal activities after being bathed in boiling water for 5 min. Acrystalliferous mutants of Bt9816C (Bt9816C-NP1 and Bt9816C-NP2) cured of its endogenous plasmids no longer possessed vip3A gene and toxicity. The 89 kD protein which existed in Bt9816C supernatant disappeared in the two mutants' supernatant; nevertheless, the two mutants still exhibited hemolytic and phospholipase C activity as Bt9816C did. The vip3A gene of Bt9816C, vip3Aa18, was cloned and expressed in Escherichia coli BL21. Bioassay demonstrated that the recombinant E. coli had high toxicity against S. exigua. Taken together, it suggested that Vip3A protein was responsible for the toxicity of Bt9816C culture supernatants.
@article{
 title = {Vip3A is responsible for the potency of <i>Bacillus thuringiensis</i> 9816C culture supernatant against Helicoverpa armigera and Spodoptera exigua.},
 type = {article},
 year = {2006},
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 keywords = {Animals,Bacillus thuringiensis,Bacillus thuringiensis: genetics,Bacillus thuringiensis: metabolism,Bacterial Proteins,Bacterial Proteins: biosynthesis,Bacterial Proteins: chemistry,Bacterial Proteins: genetics,Bacterial Proteins: physiology,Insects,Insects: microbiology,Spodoptera,Spodoptera: microbiology},
 pages = {83-89},
 volume = {52},
 websites = {http://www.ncbi.nlm.nih.gov/pubmed/16778351},
 month = {4},
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 abstract = {Culture supernatant of Bacillus thuringiensis 9816C had high toxicity against Helicoverpa armigera and Spodoptera exigua. However, it lost insecticidal activities after being bathed in boiling water for 5 min. Acrystalliferous mutants of Bt9816C (Bt9816C-NP1 and Bt9816C-NP2) cured of its endogenous plasmids no longer possessed vip3A gene and toxicity. The 89 kD protein which existed in Bt9816C supernatant disappeared in the two mutants' supernatant; nevertheless, the two mutants still exhibited hemolytic and phospholipase C activity as Bt9816C did. The vip3A gene of Bt9816C, vip3Aa18, was cloned and expressed in Escherichia coli BL21. Bioassay demonstrated that the recombinant E. coli had high toxicity against S. exigua. Taken together, it suggested that Vip3A protein was responsible for the toxicity of Bt9816C culture supernatants.},
 bibtype = {article},
 author = {Cai, Jun and Xiao, Liang and Yan, Bing and Bin, Guan and Chen, Yuehua and Ren, Gaixin},
 journal = {The Journal of General and Applied Microbiology},
 number = {2}
}
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