scholarly journals Vip3A is responsible for the potency of Bacillus thuringiensis 9816C culture supernatant against Helicoverpa armigera and Spodoptera exigua

2006 ◽  
Vol 52 (2) ◽  
pp. 83-89 ◽  
Author(s):  
Jun Cai ◽  
Liang Xiao ◽  
Bing Yan ◽  
Guan Bin ◽  
Yuehua Chen ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Helicoverpa Armigera ◽  
Spodoptera Exigua ◽  
Culture Supernatant ◽  
Helicoverpa Armígera

scholarly journals Common Receptor for Bacillus thuringiensis Toxins Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera, Helicoverpa zea, and Spodoptera exigua

2005 ◽  
Vol 71 (9) ◽  
pp. 5627-5629 ◽  
Author(s):  
Carmen Sara Hernández ◽  
Juan Ferré
Keyword(s):  
Bacillus Thuringiensis ◽  
Helicoverpa Armigera ◽  
Helicoverpa Zea ◽  
Spodoptera Exigua ◽  
Cross Resistance ◽  
Binding Studies ◽  
Lepidopteran Species ◽  
Common Receptor ◽  
Binding Data ◽  
Helicoverpa Armígera

ABSTRACT Binding studies using 125I-Cry1Ac and biotinylated Cry1Fa toxins indicate the occurrence of a common receptor for Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera, Helicoverpa zea, and Spodoptera exigua. Our results, along with previous binding data and the observed cases of cross-resistance, suggest that this pattern seems to be widespread among lepidopteran species.

scholarly journals Bacillus thuringiensis Bel Protein Enhances the Toxicity of Cry1Ac Protein to Helicoverpa armigera Larvae by Degrading Insect Intestinal Mucin

2009 ◽  
Vol 75 (16) ◽  
pp. 5237-5243 ◽  
Author(s):  
Shangling Fang ◽  
Li Wang ◽  
Wei Guo ◽  
Xia Zhang ◽  
Donghai Peng ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Helicoverpa Armigera ◽  
Trichoplusia Ni ◽  
Knockout Mutant ◽  
Gene Encoding ◽  
In Vitro Degradation ◽  
Intestinal Mucin ◽  
Helicoverpa Armígera ◽  
Cry1ac Protein

ABSTRACT Bacillus thuringiensis has been used as a bioinsecticide to control agricultural insects. Bacillus cereus group genomes were found to have a Bacillus enhancin-like (bel) gene, encoding a peptide with 20 to 30% identity to viral enhancin protein, which can enhance viral infection by degradation of the peritrophic matrix (PM) of the insect midgut. In this study, the bel gene was found to have an activity similar to that of the viral enhancin gene. A bel knockout mutant was constructed by using a plasmid-free B. thuringiensis derivative, BMB171. The 50% lethal concentrations of this mutant plus the cry1Ac insecticidal protein gene were about 5.8-fold higher than those of the BMB171 strain. When purified Bel was mixed with the Cry1Ac protein and fed to Helicoverpa armigera larvae, 3 μg/ml Cry1Ac alone induced 34.2% mortality. Meanwhile, the mortality rate rose to 74.4% when the same amount of Cry1Ac was mixed with 0.8 μg/ml of Bel. Microscopic observation showed a significant disruption detected on the midgut PM of H. armigera larvae after they were fed Bel. In vitro degradation assays showed that Bel digested the intestinal mucin (IIM) of Trichoplusia ni and H. armigera larvae to various degrading products, similar to findings for viral enhancin. These results imply Bel toxicity enhancement depends on the destruction of midgut PM and IIM, similar to the case with viral enhancin. This discovery showed that Bel has the potential to enhance insecticidal activity of B. thuringiensis-based biopesticides and transgenic crops.

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