Aedes aegypti alkaline phosphatase ALP1 is a functional receptor of Bacillus thuringiensis Cry4Ba and Cry11Aa toxins
| Autor: | Esmeralda Z. Reyes, Angeles Cancino-Rodezno, Luis Felipe Muriel-Millán, Alejandra Bravo, Sarjeet S. Gill, Supaporn Likitvivatanavong, Gustavo Caballero-Flores, Mario Soberón, Leidy Patricia Bedoya-Pérez, Alan I. Jiménez |
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| Rok vydání: | 2012 |
| Předmět: |
Insecticides
animal structures Mutant Aedes aegypti Biology Biochemistry Article Microbiology Hemolysin Proteins Western blot Bacterial Proteins RNA interference Aedes Bacillus thuringiensis medicine Gene silencing Animals Gene Silencing Molecular Biology medicine.diagnostic_test Bacillus thuringiensis Toxins fungi biology.organism_classification Alkaline Phosphatase Endotoxins RNA silencing Insect Science Larva Alkaline phosphatase Insect Proteins |
| Zdroj: | Insect biochemistry and molecular biology. 42(9) |
| ISSN: | 1879-0240 |
| Popis: | Bacillus thuringiensis subs. israelensis produces at least three Cry toxins (Cry4Aa, Cry4Ba, and Cry11Aa) that are active against Aedes aegypti larvae. Previous work characterized a GPI-anchored alkaline phosphatase (ALP1) as a Cry11Aa binding molecule from the gut of A. aegypti larvae. We show here that Cry4Ba binds ALP1, and that the binding and toxicity of Cry4Ba mutants located in loop 2 of domain II is correlated. Also, we analyzed the contribution of ALP1 towards the toxicity of Cry4Ba and Cry11Aa toxins by silencing the expression of this protein though RNAi. Efficient silencing of ALP1 was demonstrated by real-time quantitative PCR (qPCR) and Western blot. ALP1 silenced larvae showed tolerance to both Cry4Ba and Cry11Aa although the silenced larvae were more tolerant to Cry11Aa in comparison to Cry4Ba. Our results demonstrate that ALP1 is a functional receptor that plays an important role in the toxicity of the Cry4Ba and Cry11Aa proteins. |
| Databáze: | OpenAIRE |
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