Effects of midgut-protein-preparative and ligand binding procedures on the toxin binding characteristics of BT-R1, a common high-affinity receptor in Manduca sexta for Cry1A Bacillus thuringiensis toxins

Article Abstract:

A study was conducted to analyze the influence of midgut-protein-preparative and ligand binding steps on the toxin binding features of a high-affinity receptor in Manduca sexta for Cry1A Bacillus thuringiensis toxins. Total protein was determined using the bicinchoninic acid technique while midguts were homogenized in ice-cold buffer volumes characterized by mannitol and a Tris base. Results suggested that the toxins act through a common receptor and a common mode of action in M. sexta.

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Ligand specificity and affinity of BT-R, the Bacillus thuringiensis Cry1A toxin receptor from Manduca sexta, expressed in mammalian and insect cell cultures

Article Abstract:

Microbiological research has identified the ligand binding characteristics of the Manduca sexta receptor BT-R1 for the Bacillus thuringiensis Cry1Aa, Cry1Ab and Cry1Ac toxins. The BT-R1 receptor is the first of its kind to be functionally expressed in heterologous cell cultures. Competition binding assays were performed to establish BT-R1 affinity and specificity for lepidopteran-specific Cry1Ab toxin.

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Partial purification and characterization of Bacillus thuringiensis Cry1A toxin receptor A from Heliothis virescens and cloning of the corresponding cDNA

Article Abstract:

Research is conducted on the Heliothis virescens molecular structure identified as a Cry1A toxin-binding protein and receptor A. Experiments suggest that Cry1A toxin interactions can be affected by posttranslational modifications.

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