ArticlePloS one2014
Structural and biophysical characterization of Bacillus thuringiensis insecticidal proteins Cry34Ab1 and Cry35Ab1.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.
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Who cites it
34 citing papers in PubMed, 1 synthesis or guideline pooled it, 74 citations in OpenAlex.
- Sequential evolution of resistance by western corn rootworm to multipleProceedings of the National Academy of Sciences of the United States of America · 2025Pooled it
- Unveiling Putative Functions of Burkholderia pseudomallei K96243 Hypothetical Proteins Via High-Throughput Characterization of Structural Similarities.Interdisciplinary sciences, computational life sciences · 2026Article
- Identification, expression, and insecticidal activity analysis of a novel cry toxin gene from Bacillus thuringiensis Gxun777-1.World journal of microbiology & biotechnology · 2026Article
- The Biological Role of Conoporins, Actinoporin-like Pore-Forming Toxins from Cone Snails.Toxins · 2025Review
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Inheritance and Fitness Costs of Laboratory-Selected Resistance to Gpp34/Tpp35Ab1 Corn in Western Corn Rootworm (Coleoptera: Chrysomelidae).Journal of economic entomology · 2023Article
- Towards Understanding the Function of Aegerolysins.Toxins · 2022Review
- The crystal structure of Cry78Aa from Bacillus thuringiensis provides insights into its insecticidal activity.Communications biology · 2022Article
- Towards a Fungal Science That Is Independent of Researchers' Gender.Journal of fungi (Basel, Switzerland) · 2022Article
- Engineering of Cry3Bb1 provides mechanistic insights toward countering western corn rootworm resistance.Current research in insect science · 2022Article
- Proteomic and metabolomic approach to rationalize the differential mosquito larvicidal toxicity inAnalytical science advances · 2021Article
- Lipid-Binding Aegerolysin from Biocontrol FungusToxins · 2021Article
- Review
- Effects of Bioinsecticidal Aegerolysin-Based Cytolytic Complexes on Non-Target Organisms.Toxins · 2021Article
- Article
- How DoesToxins · 2021Review
- Crystal structure of RahU, an aegerolysin protein from the human pathogen Pseudomonas aeruginosa, and its interaction with membrane ceramide phosphorylethanolamine.Scientific reports · 2021Article
- Article
- Whole Genome Sequencing Analysis ofFrontiers in microbiology · 2021Article
- The Cry48Aa N-terminal Domain is Responsible for Cry48Aa-Cry49Aa Interaction in Lysinibacillus sphaericus Toxin.Current microbiology · 2020Article
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Authors and funding
13 authors at 1 institution in 1 country.
Funding
Abstract
Bacillus thuringiensis strains are well known for the production of insecticidal proteins upon sporulation and these proteins are deposited in parasporal crystalline inclusions. The majority of these insect-specific toxins exhibit three domains in the mature toxin sequence. However, other Cry toxins are structurally and evolutionarily unrelated to this three-domain family and little is known of their three dimensional structures, limiting our understanding of their mechanisms of action and our ability to engineer the proteins to enhance their function. Among the non-three domain Cry toxins, the Cry34Ab1 and Cry35Ab1 proteins from B. thuringiensis strain PS149B1 are required to act together to produce toxicity to the western corn rootworm (WCR) Diabrotica virgifera virgifera Le Conte via a pore forming mechanism of action. Cry34Ab1 is a protein of ∼14 kDa with features of the aegerolysin family (Pfam06355) of proteins that have known membrane disrupting activity, while Cry35Ab1 is a ∼44 kDa member of the toxin_10 family (Pfam05431) that includes other insecticidal proteins such as the binary toxin BinA/BinB. The Cry34Ab1/Cry35Ab1 proteins represent an important seed trait technology having been developed as insect resistance traits in commercialized corn hybrids for control of WCR. The structures of Cry34Ab1 and Cry35Ab1 have been elucidated to 2.15 Å and 1.80 Å resolution, respectively. The solution structures of the toxins were further studied by small angle X-ray scattering and native electrospray ion mobility mass spectrometry. We present here the first published structure from the aegerolysin protein domain family and the structural comparisons of Cry34Ab1 and Cry35Ab1 with other pore forming toxins.
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