An ADAM metalloprotease is a Cry3Aa Bacillus thuringiensis toxin receptor
| Autor: | Carolina Rausell, Camila Ochoa-Campuzano, Alejandra Bravo, Amparo C. Martínez-Ramírez, M. Dolores Real |
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| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular ADAM10 Bacterial Toxins Molecular Sequence Data Biophysics medicine.disease_cause Biochemistry Substrate Specificity Hemolysin Proteins Bacterial Proteins Sequence Analysis Protein Bacillus thuringiensis medicine Animals Electrophoresis Gel Two-Dimensional Amino Acid Sequence Mode of action Receptor Molecular Biology Fluorescent Dyes Metalloproteinase Binding Sites biology Bacillus thuringiensis Toxins Microvilli Sequence Homology Amino Acid Toxin Colorado potato beetle Cell Membrane Cell Biology biology.organism_classification Molecular biology Protein Structure Tertiary carbohydrates (lipids) Blot Coleoptera Endotoxins ADAM Proteins Insect Proteins Carrier Proteins Oligopeptides Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 362(2) |
| ISSN: | 0006-291X |
| Popis: | Bacillus thuringiensis insecticidal proteins toxic action relies on the interaction with receptor molecules on insect midgut target cells. Here, we describe an ADAM metalloprotease as a novel type of B. thuringiensis toxin receptor on the basis of the following data: (i) by ligand blot and N-terminal analysis, we detected a Colorado potato beetle Cry3Aa toxin binding molecule that shares homology with an ADAM10 metalloprotease; (ii) Colorado potato beetle brush border membrane vesicles display ADAM activity since it cleaves an ADAM fluorogenic substrate; (iii) Cry3Aa acts as a competitor of the cleavage of the ADAM fluorogenic substrate; (iv) Cry3Aa sequence contains the recognition motif R(345)FQPGYYGND(354) present in ADAM10 substrates. Accordingly, a peptide representative of the recognition motif localized within loop 1 of Cry3Aa domain II (Ac-F(341)HTRFQPGYYGNDSFN(358)-NH(2)) effectively prevented Cry3Aa proteolytic processing and nearly abolished pore formation, evidencing the functional significance of the Cry3Aa-ADAM interaction in relation to this toxin mode of action. |
| Databáze: | OpenAIRE |
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