Li, J., Koni, P.A. and Ellar, D.J. (1996) Structure of the Mosquitocidal δ-Endotoxin CytB from Bacillus thuringiensissp. Kyushuensis and Implications for Membrane Pore Formation. Journal of Molecular Biology, 257, 129-152.
https://doi.org/10.1006/jmbi.1996.0152

has been cited by the following article:

• TITLE: Characterization of the Novel Insecticidal Crystal Protein Cyt3Aa1 from Bacillus thuringiensis TD516

  AUTHORS: Jun Zhu, Zizhong Zhu, Baoli Zhang, Xu Liu, Yiping Liu, Aiping Zheng, Shiquan Wang, Shuangcheng Li, Qiming Deng, Huainian Liu, Yueyang Liang, Ting Zou, Aijun Wang, Lingxia Wang, Ping Li

  KEYWORDS: TD516, Cyt3Aa1, Activity Assays, Three-Dimensional Structure

  JOURNAL NAME: Advances in Microbiology, Vol.10 No.7, July 24, 2020

  ABSTRACT: Bacillus thuringiensis (Bt) produces two families of insecticidal crystal proteins, i.e., crystalline (Cry) and cytolytic (Cyt) toxins. Cyt3Aa1, the newest Cyt family member, is produced by Bt TD516. Bioassay results have shown that Cyt3Aa1 has weak hemolytic activity against human red blood cells and is not toxic to A. aegypti larvae, but causing a teratogenic effect. The three-dimensional structure of Cyt3Aa1 has a typical cytolysin fold containing a β-sheet held by two surrounding α-helical layers, resembling the previously reported Cyt1Aa and Cyt2Aa structures, which indicated that Cyt3Aa1 might be a membrane-perforation toxin and could induce synergism with Cry protein. This study provides a new source of insecticidal crystal proteins, and presents a foundation for understanding the biological characterization of it, which will aid in the development of strategies to cope with the potential problem of insect resistance.