Structural basis for the assembly and translocation of the Vip1-Vip2 insecticidal toxin from Bacillus thuringiensis - PubMed
6 hours ago
- #Bacillus thuringiensis
- #cryo-EM
- #insecticidal toxin
- Study presents cryo-EM structures of heptameric Vip1-pore and Vip2-bound Vip1-pore complex from Bacillus thuringiensis.
- Identifies putative assembly intermediates, suggesting a sequential assembly and sequence-independent translocation pathway for the binary toxin.
- Structure-guided mutagenesis provides insights into the mechanism, and proof-of-concept shows protein delivery into host cells using mini-Vip2-Vip1 pore system.
- Findings clarify the toxin's mode of action and offer a model for studying human-pathogenic pore-forming toxins due to similarity and biosafety.