<i>Bacillus thuringiensis</i> Cry4Ba Insecticidal ToxinExploits Leu<sup>615</sup> in Its C-Terminal Domain to Interact with a Target Receptor—<i>Aedes aegypti</i> Membrane-Bound Alkaline Phosphatase

<i>Bacillus thuringiensis</i> Cry4Ba Insecticidal ToxinExploits Leu<sup>615</sup> in Its C-Terminal Domain to Interact with a Target Receptor—<i>Aedes aegypti</i> Membrane-Bound Alkaline Phosphatase

In addition to the receptor-binding domain (DII), the C-terminal domain (DIII) of three-domain Cry insecticidal δ-endotoxins from <i>Bacillus thuringiensis</i> has been implicated in target insect specificity, yet its precise mechanistic role remains unclear. Here, the 21 kDa high-purity...

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Bibliographic Details
Main Authors:	Anon Thammasittirong, Sutticha Na-Ranong Thammasittirong, Chompounoot Imtong, Sathapat Charoenjotivadhanakul, Somsri Sakdee, Hui-Chun Li, Siriporn Okonogi, Chanan Angsuthanasombat
Format:	Article
Language:	English
Published:	MDPI AG 2021-08-01
Series:	Toxins
Subjects:	Cry4Ba mosquito-active toxin enzyme-linked immunosorbent assay GPI-anchored alkaline phosphatase homology-based modeling molecular docking receptor binding
Online Access:	https://www.mdpi.com/2072-6651/13/8/553

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