A membrane associated metalloprotease cleaves Cry3Aa Bacillus thuringiensis toxin reducing pore formation in Colorado potato beetle brush border membrane vesicles
| Autor: | Alejandra Bravo, María Dolores Real, Amparo C. Martínez-Ramírez, Carolina Rausell, Camila Ochoa-Campuzano |
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| Rok vydání: | 2007 |
| Předmět: |
Proteases
Cell Membrane Permeability Pore formation Proteolysis medicine.medical_treatment Bacterial Toxins Bacillus thuringiensis Biophysics Insecticidal toxin Biochemistry Cry3Aa proteolysis Hemolysin Proteins Bacterial Proteins medicine Colorado potato beetle Animals Metalloprotease inhibitor Metalloproteinase Binding Sites Protease Bacillus thuringiensis Toxins Microvilli biology medicine.diagnostic_test Secretory Vesicles Acetohydroxamic acid Cell Biology biology.organism_classification Coleoptera Endotoxins Models Chemical Porosity Protein Binding medicine.drug |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1768:2293-2299 |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/j.bbamem.2007.06.014 |
| Popis: | Insect proteases are implicated in Bacillus thuringiensis insecticidal proteins mode of action determining toxin specificity and sensitivity. Few data are available on the involvement of proteases in the later steps of toxicity such as protease interaction with toxin–receptor complexes and the pore formation process. In this study, a Colorado potato beetle (CPB) midgut membrane metalloprotease was found to be involved in the proteolytic processing of Cry3Aa. Interaction of Cry3Aa with BBMV membrane proteases resulted in a distinct pattern of proteolysis. Cleavage was demonstrated to occur in protease accessible regions of domain III and was specifically inhibited by the metalloprotease inhibitors 1,10-phenanthroline and acetohydroxamic acid. Proteolytic inhibition by a peptide representing a segment of proteolysis in domain III and the metalloprotease inhibitor acetohydroxamic acid correlated with increased pore formation, evidencing that Cry3Aa is a specific target of a CPB membrane metalloprotease that degrades potentially active toxin. |
| Databáze: | OpenAIRE |
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