The Vip3Ag4 Insecticidal Protoxin from Bacillus thuringiensis Adopts A Tetrameric Configuration That Is Maintained on Proteolysis

Toxins
Leopoldo PalmaColin Berry

Abstract

The Vip3 proteins produced during vegetative growth by strains of the bacteriumBacillus thuringiensisshow insecticidal activity against lepidopteran insects with a mechanism of action that may involve pore formation and apoptosis. These proteins are promising supplements to our arsenal of insecticidal proteins, but the molecular details of their activity are not understood. As a first step in the structural characterisation of these proteins, we have analysed their secondary structure and resolved the surface topology of a tetrameric complex of the Vip3Ag4 protein by transmission electron microscopy. Sites sensitive to proteolysis by trypsin are identified and the trypsin-cleaved protein appears to retain a similar structure as an octomeric complex comprising four copies each of the ~65 kDa and ~21 kDa products of proteolysis. This processed form of the toxin may represent the active toxin. The quality and monodispersity of the protein produced in this study make Vip3Ag4 a candidate for more detailed structural analysis using cryo-electron microscopy.

References

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Citations

Dec 27, 2017·Toxins·Alexey S Ladokhin
Dec 17, 2019·Protein Science : a Publication of the Protein Society·Meiying ZhengJeff Haas
Aug 10, 2020·Nature Communications·Rafael Núñez-RamírezErnesto Arias-Palomo
Jan 9, 2021·Annual Review of Entomology·Juan Luis Jurat-FuentesJuan Ferré
Sep 4, 2017·Biochimica Et Biophysica Acta. Biomembranes·Thittaya KunthicPanadda Boonserm
May 16, 2021·Nature Communications·Matthew J ByrneRebecca F Thompson
Nov 29, 2021·Molecular Biology Reports·Mohsin ShadAhmad Ali Shahid

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Methods Mentioned

BETA
transgenic
transmission electron microscopy
gel filtration
Size exclusion chromatography
circular dichroism
light
dynamic

Software Mentioned

SEDNTERP
SEDFIT
EMAN2
CONTIN
EMAN

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