ArticleNature communications2020
Serial femtosecond crystallography on in vivo-grown crystals drives elucidation of mosquitocidal Cyt1Aa bioactivation cascade.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- NativeJournal of tropical medicine · 2026Article
- Oligomer assembly ofToxicon: X · 2025Article
- A snapshot love story: what serial crystallography has done and will do for us.Acta crystallographica. Section D, Structural biology · 2024Review
- RecombinantMicrobiology spectrum · 2024Article
- Review
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Channel Formation in Cry Toxins: An Alphafold-2 Perspective.International journal of molecular sciences · 2023Article
- The Parasporal Body ofBiology · 2023Article
- Review of serial femtosecond crystallography including the COVID-19 pandemic impact and future outlook.Structure (London, England : 1993) · 2023Review
- Going around the Kok cycle of the water oxidation reaction with femtosecond X-ray crystallography.IUCrJ · 2023Article
- Structural insights into functional properties of the oxidized form of cytochrome c oxidase.Nature communications · 2023Article
- Mutation of a Threonine Residue in αD-β4 Loop of Cyt2Aa2 Protein Influences Binding on Fluid Lipid Membranes.Toxins · 2023Article
- Cell-free protein crystallization for nanocrystal structure determination.Scientific reports · 2022Article
- Serial femtosecond crystallography.Nature reviews. Methods primers · 2022Article
- De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals.Nature communications · 2022Article
- Review
- How DoesToxins · 2021Review
- Can (We Make)Toxins · 2021Review
- In vivo nanoscale analysis of the dynamic synergistic interaction of Bacillus thuringiensis Cry11Aa and Cyt1Aa toxins in Aedes aegypti.PLoS pathogens · 2021Article
- Dynamic Structural Biology Experiments at XFEL or Synchrotron Sources.Methods in molecular biology (Clifton, N.J.) · 2021Review
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38 authors.
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Abstract
Cyt1Aa is the one of four crystalline protoxins produced by mosquitocidal bacterium Bacillus thuringiensis israelensis (Bti) that has been shown to delay the evolution of insect resistance in the field. Limiting our understanding of Bti efficacy and the path to improved toxicity and spectrum has been ignorance of how Cyt1Aa crystallizes in vivo and of its mechanism of toxicity. Here, we use serial femtosecond crystallography to determine the Cyt1Aa protoxin structure from sub-micron-sized crystals produced in Bti. Structures determined under various pH/redox conditions illuminate the role played by previously uncharacterized disulfide-bridge and domain-swapped interfaces from crystal formation in Bti to dissolution in the larval mosquito midgut. Biochemical, toxicological and biophysical methods enable the deconvolution of key steps in the Cyt1Aa bioactivation cascade. We additionally show that the size, shape, production yield, pH sensitivity and toxicity of Cyt1Aa crystals grown in Bti can be controlled by single atom substitution.
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