Binding Analysis of Sf-SR-C MAM Domain and Sf-FGFR Ectodomain to Vip3Aa

<i>Bacillus thuringiensis</i> Vip3Aa has been widely used in transgenic crops to resist the erosion of insects. The Scavenger Receptor-C (SR-C) and Fibroblast Growth Factor Receptor (FGFR) of <i>Spodoptera frugiperda</i> (Sf-SR-C and Sf-FGFR) have formerly been identified as...

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Bibliographic Details
Published in:Insects
Main Authors: Chenghai Wang, Min Li, Xiling Chen, Shilong Fan, Jun Lan
Format: Article
Language:English
Published: MDPI AG 2024-06-01
Subjects:
Vip3Aa
Sf-SR-C
Sf-FGFR
crystal structure
SPR
structure docking
Online Access:https://www.mdpi.com/2075-4450/15/6/428
Description
Summary:<i>Bacillus thuringiensis</i> Vip3Aa has been widely used in transgenic crops to resist the erosion of insects. The Scavenger Receptor-C (SR-C) and Fibroblast Growth Factor Receptor (FGFR) of <i>Spodoptera frugiperda</i> (Sf-SR-C and Sf-FGFR) have formerly been identified as the cell receptors of Vip3Aa. However, the interaction mechanism of Vip3Aa binding to Sf-SR-C or Sf-FGFR is still unknown. Here, we purified the MAM domain of Sf-SR-C (Sf-MAM) and the Sf-FGFR ectodomain expressed extracellularly by Sf9 cells. We then solved the crystal structure of the Sf-MAM domain. Structure docking analysis of the Sf-MAM and Vip3Aa C-terminal domain (CTD) excluded the possibility of the two proteins binding. A further surface plasmon resonance (SPR) assay also revealed that the Sf-MAM and Sf-FGFR ectodomain could not bind to the Vip3Aa protein. Our results have raised the urgency of determining the authentic cell receptor for Vip3Aa.
ISSN:2075-4450

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