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Updated: Oct 24, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Structure and functional divergence of the non-canonical BoNT-like toxin PG1 and PG2
JinBo Yang1, Zheng Liu2,3,4, Linlin Jiang5
1Institute of Future Agriculture, Northwest Agriculture and Forestry University, Yangling, Shaanxi, 712100, China.
Abstract:
Botulinum neurotoxins (BoNTs) are potent bacterial toxins. Distinct BoNT-like toxins, including BoNT/X, BoNT/En, and PMP1, form a distinct lineage. Here we characterize two additional members of this group, PG-toxin 1 and 2 (PG1 and PG2). Their light-chain (LC) and heavy-chain (HC) domains are encoded by adjacent genes. PG1 and PG2 LCs cleave Drosophila SNAP-25 at distinct sites (N196-E197 and R191-K193, respectively); PG1 is more potent, while PG2 activity depends on pH and ionic strength. Both LCs enter Sf9 cells via clathrin-mediated endocytosis. PG1 LC is toxic to Drosophila and northern armyworm independently of its HC, whereas PG2 LC toxicity is enhanced by its HC. Cryo-EM shows that PG1 adopts a distinct compact di-chain architecture with a door-hinge-like "belt." These findings expand the structural and functional diversity of the BoNT family and support the potential of PG-toxins as insecticidal agents and research tools.
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