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Peer-reviewedCC BY-NC-NDNature communications

Structure and functional divergence of the non-canonical BoNT-like toxin PG1 and PG2.

  • JinBo Yang1
  • Zheng Liu2,3,4
  • Linlin Jiang5
  • Xiaoyan Ye1
  • Yuwen Chao2,3,4
  • Jing Ren2,3,4
  • Xiaofeng Zhu1
  • Shaoyu Yang1
  • Xinyuan Guo1
  • Ji Zeng6
  • Hua Wu5,7
  • Peng Chen8,9,10
1 more authors
  • Sicai Zhang11
11 affiliations
  1. 1Institute of Future Agriculture, Northwest Agriculture and Forestry University, Yangling, Shaanxi, 712100, China.
  2. 2Department of Hepatobiliary and Pancreatic Surgery, Zhongnan Hospital of Wuhan University, Taikang Center for Life and Medical Sciences, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
  3. 3Clinical Medicine Research Center for Minimally Invasive Procedure of Hepatobiliary & Pancreatic Diseases of Hubei Province, Hubei, China.
  4. 4Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
  5. 5Key Laboratory of Plant Protection Resources and Pest Management of Ministry of Education, College of Plant Protection, Northwest A & F University, Yangling, Shaanxi, 712100, China.
  6. 6School of Biomedical and Pharmaceutical Sciences, Guangdong University of Technology, Guangzhou, 510006, China.
  7. 7Shaanxi Province Center for Bio-Pesticide Engineering, Yangling, 712100, China.
  8. 8Department of Hepatobiliary and Pancreatic Surgery, Zhongnan Hospital of Wuhan University, Taikang Center for Life and Medical Sciences, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China. [email protected].
  9. 9Clinical Medicine Research Center for Minimally Invasive Procedure of Hepatobiliary & Pancreatic Diseases of Hubei Province, Hubei, China. [email protected].
  10. 10Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China. [email protected].
  11. 11Institute of Future Agriculture, Northwest Agriculture and Forestry University, Yangling, Shaanxi, 712100, China. [email protected].
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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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Cite

BibTeXRIS
BibTeX
@article{yang2026structure,
  title = {{Structure and functional divergence of the non-canonical BoNT-like toxin PG1 and PG2.}},
  author = {JinBo Yang and Zheng Liu and Linlin Jiang and Xiaoyan Ye and Yuwen Chao and Jing Ren and Xiaofeng Zhu and Shaoyu Yang and Xinyuan Guo and Ji Zeng and Hua Wu and Peng Chen and Sicai Zhang},
  journal = {Nature communications},
  year = {2026},
  month = sep,
  doi = {10.1038/s41467-026-77991-2},
  url = {https://europepmc.org/article/MED/42907452},
  note = {CC BY-NC-ND},
}
RIS
TY  - JOUR
TI  - Structure and functional divergence of the non-canonical BoNT-like toxin PG1 and PG2.
AU  - JinBo Yang
AU  - Zheng Liu
AU  - Linlin Jiang
AU  - Xiaoyan Ye
AU  - Yuwen Chao
AU  - Jing Ren
AU  - Xiaofeng Zhu
AU  - Shaoyu Yang
AU  - Xinyuan Guo
AU  - Ji Zeng
AU  - Hua Wu
AU  - Peng Chen
AU  - Sicai Zhang
PY  - 2026
DA  - 2026/09/22
JO  - Nature communications
DO  - 10.1038/s41467-026-77991-2
UR  - https://europepmc.org/article/MED/42907452
AB  - 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.
SN  - 2041-1723
ER  -