Lee, P.G., Yin, L., Wei, X., Shi, J., Masuyer, G., Wentz, T.G., Chen, P., Xu, Y., Liang, J., Zhang, H., Persson Košenina, S., Lobb, B., Mansfield, M., Gill, S.S., Pellett, S., Stenmark, P., Doxey, A.C., Dong, M. (2025). Identification and characterization of botulinum neurotoxin-like two-component toxins in Paeniclostridium ghonii.  Sci. Adv. 11(46): eadx6145.

FBrf0263809

Research paper

Insecticidal bacterial proteins play key roles in insect-bacteria interactions and have been used as biopesticides. Here, we identify two insecticidal proteins in Paeniclostridium ghonii, designated PG-toxin 1 (PG1) and PG-toxin 2 (PG2), which are homologs of botulinum neurotoxins (BoNTs). Unlike BoNTs, PG1 and PG2 contain two separate proteins: One is the protease light chain (LC), and the other is the heavy chain containing the translocation domain and the receptor binding domain. Crystal and cryo-electron microscopy structures show a conserved BoNT-like architecture but without an interchain disulfide bond. Functional characterizations establish that the LCs of PG1 and PG2 cleave insect synaptosomal-associated protein 25 (SNAP25), but not human or rat SNAP25, and microinjection of PG1 and PG2 caused paralysis and death in Drosophila and Aedes mosquitoes. These findings identified unique two-component BoNT-like insecticidal proteins, revealing insights into the evolution of the BoNT family of toxins, and broadening our understanding of bacteria that can be used for biopest controls.

PMC12609057 (PMC) (EuropePMC)