ArticleAMB Express2021
Key residues of Bacillus thuringiensis Cry2Ab for oligomerization and pore-formation activity.
Article in AMB Express, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Article
- Bioactive Potential of SomeInsects · 2024Article
- Article
- V-ATPase C Acts as a Receptor forInsects · 2024Article
- N-Terminal α-Helices in Domain I ofToxins · 2024Article
- Engineering of Bacillus thuringiensis Cry2Ab toxin for improved insecticidal activity.AMB Express · 2024Article
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Authors and funding
5 authors.
Funding
Abstract
As a pore-forming toxin, activation, oligomerization and pore-formation were both required for the mode of action of Cry toxins. Previous results revealed that the helices α4-α5 of Domain I were involved in the oligomerization of Cry2Ab, however, the key residues for Cry2Ab aggregation remained ambiguous. In present studies, we built 20 Cry2Ab alanine mutants site-directed in the helices α4-α5 of Domain I and demonstrated that mutants N151A, T152A, F157A, L183A, L185A and I188A could reduce the assembly of the 250 kDa oligomers, suggesting that these mutation residues might be essential for Cry2Ab oligomerization. As expected, all of these variants showed lower insecticidal activity against P. xylostella. Furthermore, we found that the pore-forming activities of these mutants also decreased when compared to wild-type Cry2Ab. Taken together, our data identified key residues for Cry2Ab oligomerization and emphasized that oligomerization was closely related to the insecticidal activity and pore-forming activity of Cry2Ab.
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