Bacillus thuringiensis Cry4Ba Insecticidal ToxinExploits Leu⁶¹⁵ in Its C-Terminal Domain to Interact with a Target Receptor-Aedes aegypti Membrane-Bound Alkaline Phosphatase.

ABSTRACT: In addition to the receptor-binding domain (DII), the C-terminal domain (DIII) of three-domain Cry insecticidal δ-endotoxins from Bacillus thuringiensis has been implicated in target insect specificity, yet its precise mechanistic role remains unclear. Here, the 21 kDa high-purity isolated DIII fragment derived from the Cry4Ba mosquito-specific toxin was achieved via optimized preparative FPLC, allowing direct rendering analyses for binding characteristics toward its target receptor-Aedes aegypti membrane-bound alkaline phosphatase (Aa-mALP). Binding analysis via dotblotting revealed that the Cry4Ba-DIII truncate was capable of specific binding to nitrocellulose-bound Aa-mALP, with a binding signal comparable to its 65 kDa Cry4Ba-R203Q full-length toxin. Further determination

SUBMITTER: Thammasittirong A 

PROVIDER: S-EPMC8402544 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature