Bacillus thuringiensis Crystal Protein Cry6Aa Triggers Caenorhabditis elegans Necrosis Pathway Mediated by Aspartic Protease (ASP-1)

PLoS Pathogens
Fengjuan ZhangM Sun

Abstract

Cell death plays an important role in host-pathogen interactions. Crystal proteins (toxins) are essential components of Bacillus thuringiensis (Bt) biological pesticides because of their specific toxicity against insects and nematodes. However, the mode of action by which crystal toxins to induce cell death is not completely understood. Here we show that crystal toxin triggers cell death by necrosis signaling pathway using crystal toxin Cry6Aa-Caenorhabditis elegans toxin-host interaction system, which involves an increase in concentrations of cytoplasmic calcium, lysosomal lyses, uptake of propidium iodide, and burst of death fluorescence. We find that a deficiency in the necrosis pathway confers tolerance to Cry6Aa toxin. Intriguingly, the necrosis pathway is specifically triggered by Cry6Aa, not by Cry5Ba, whose amino acid sequence is different from that of Cry6Aa. Furthermore, Cry6Aa-induced necrosis pathway requires aspartic protease (ASP-1). In addition, ASP-1 protects Cry6Aa from over-degradation in C. elegans. This is the first demonstration that deficiency in necrosis pathway confers tolerance to Bt crystal protein, and that Cry6A triggers necrosis represents a newly added necrosis paradigm in the C. elegans. Understan...Continue Reading

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Citations

Aug 20, 2016·Scientific Reports·Ziqiang ZhengMing Sun
Jul 29, 2016·Proceedings. Biological Sciences·Jinshui ZhengMing Sun
May 27, 2020·PLoS Neglected Tropical Diseases·Douglas P JasmerMakedonka Mitreva
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May 30, 2021·Developmental and Comparative Immunology·Alejandra Zárate-PotesHinrich Schulenburg

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Datasets Mentioned

BETA
AF210248

Methods Mentioned

BETA
ELISA
Isothermal titration calorimetric
dot blot
isothermal titration calorimetry
transgenic
fluorescence microscopy
FRET
electrophoresis
PCR

Software Mentioned

Origin
Olympus
Olympus cellSens
FV10
ASW
Matrix Science
cellSens

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