ArticleScientific reports2018
Helix α-3 inter-molecular salt bridges and conformational changes are essential for toxicity of Bacillus thuringiensis 3D-Cry toxin family.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Channel Formation in Cry Toxins: An Alphafold-2 Perspective.International journal of molecular sciences · 2023Article
- Structural changes upon membrane insertion of the insecticidal pore-forming toxins produced byFrontiers in insect science · 2023Review
- Genetic Modification Approaches for ParasporinsMolecules (Basel, Switzerland) · 2021Review
- Bacillus thuringiensis Cry1Ab Domain III β-16 Is Involved in Binding to Prohibitin, Which Correlates with Toxicity against Helicoverpa armigera (Lepidoptera: Noctuidae).Applied and environmental microbiology · 2021Article
- Whole Genome Sequencing Analysis ofFrontiers in microbiology · 2021Article
- Rearrangement of N-Terminal α-Helices ofToxins · 2020Article
- Oligomerization is a key step for Bacillus thuringiensis Cyt1Aa insecticidal activity but not for toxicity against red blood cells.Insect biochemistry and molecular biology · 2020Article
- Article
- Triple arginines as molecular determinants for pentameric assembly of the intracellular domain of 5-HTThe Journal of general physiology · 2019Article
- "The Defined Toxin-binding Region of the Cadherin G-protein Coupled Receptor, BT-RJournal of proteomics & bioinformatics · 2018Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Bacillus thuringiensis insecticidal Cry toxins break down larval midgut-cells after forming pores. The 3D-structures of Cry4Ba and Cry5Ba revealed a trimeric-oligomer after cleavage of helices α-1 and α-2a, where helix α-3 is extended and made contacts with adjacent monomers. Molecular dynamic simulations of Cry1Ab-oligomer model based on Cry4Ba-coordinates showed that E101 forms a salt-bridge with R99 from neighbor monomer. An additional salt bridge was identified in the trimeric-Cry5Ba, located at the extended helix α-3 in the region corresponding to the α-2b and α-3 loop. Both salt-bridges were analyzed by site directed mutagenesis. Single-point mutations in the Lepidoptera-specific Cry1Ab and Cry1Fa toxins were affected in toxicity, while reversed double-point mutant partially recovered the phenotype, consistent with a critical role of these salt-bridges. The single-point mutations in the salt-bridge at the extended helix α-3 of the nematicidal Cry5Ba were also non-toxic. The incorporation of this additional salt bridge into the nontoxic Cry1Ab-R99E mutant partially restored oligomerization and toxicity, supporting that the loop between α-2b and α-3 forms part of an extended helix α-3 upon oligomerization of Cry1 toxins. Overall, these results highlight the role in toxicity of salt-bridge formation between helices α-3 of adjacent monomers supporting a conformational change in helix α-3.
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