Nematode-specific cadherin CDH-8 acts as a receptor for Cry5B toxin in Caenorhabditis elegans
Parasitic nematodes of animals and plants cause worldwide devastating impacts on people’s lives and agricultural crops. The crystal protein Cry5B produced by Bacillus thuringiensis has efficient and specific activity against a wide range of nematodes. However, the action mode of this toxin has not yet been thoroughly determined. Here, a nematode-specific cadherin CDH-8 was demonstrated to be a receptor for Cry5B toxin by using Caenorhabditis elegans as a model, providing evidence that the cadherin mutant worm cdh-8(RB815) possesses significant resistance to Cry5B, and the CDH-8 fragments bind specifically to Cry5B. Furthermore, CDH-8 was identified to be required for the oligomerization of Cry5B toxin in vivo and contribute to the internalization and pore formation of Cry5B in nematode cells. This study will facilitate a better understanding of the action mode of nematicidal Cry toxins and help the design of Cry toxin-based products for the control of plant or animal parasitic nematodes.
KeywordsNematicidal crystal protein Caenorhabditis elegans Receptor Cadherin
We thank Professor Hanchang Zhu (College of Foreign Language, Huazhong Agricultural University, Wuhan, China) for carefully proofreading this manuscript. This study was supported by the National Key R&D Program of China (2017YFD0200400 and 2017YFD0201201), the National Natural Science Foundation of China (31770116 and 31670085), and the Fundamental Research Funds for the Central Universities (2662016PY067).
DHP and MS designed the study and wrote the manuscript. DFW, CSC, XBY, and DHP participated in the experiments. DHP and DFW analyzed the data and contributed to the figures and tables. DFW performed the bioinformatic analysis. All authors have read and approved the final manuscript.
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Conflict of interest
The authors declare that they have no conflict of interest.
This research does not contain any studies with human participants or animals.
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