Toxin-binding proteins from midgut epithelium membranes of Anopheles stephensi larvae
| Autor: | L. P. Revina, L. A. Ganushkina, M. A. Dronina, Galina G. Chestukhina, L. I. Kostina, Zalunin Ia |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Proteolysis
Bacterial Toxins Bacillus thuringiensis medicine.disease_cause Biochemistry Chromatography Affinity Hemolysin Proteins Affinity chromatography Bacterial Proteins Anopheles medicine Animals Intestinal Mucosa Receptor Peptide sequence Anopheles stephensi medicine.diagnostic_test biology Bacillus thuringiensis Toxins Microvilli Toxin fungi Midgut General Medicine biology.organism_classification Molecular biology Epithelium Phosphoric Monoester Hydrolases Endotoxins Molecular Weight medicine.anatomical_structure Larva Carrier Proteins |
| Zdroj: | Biochemistry. Biokhimiia. 71(2) |
| ISSN: | 0006-2979 |
| Popis: | Proteins of 65 and 57 kD were isolated from the apical membranes of midgut epithelium of Anopheles stephensi larvae by affinity chromatography. These proteins can specifically bind endotoxin Cry11A and activate toxin Cry4B (Cry4B-tox) under conditions of ligand blotting, and both Cry proteins compete for this binding. At least in the case of Cry4B-tox, the binding with 65 and 57 kD proteins is reversible. The ability of the products of limited proteolysis of Cry11A and Cry4B to bind the 65 and 57 kD proteins correlates with their toxicity to A. stephensi larva. The N-terminal amino acid sequence of the 57 kD protein is unique and absent in the NCBI GenBank. The proteins of 65 and 57 kD share most of the properties studied with Aedes aegypti toxin-binding proteins. It is possible that they altogether represent a novel class (or classes) of delta-endotoxin receptors. |
| Databáze: | OpenAIRE |
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