Cry11Aa and Cyt1Aa exhibit different structural orders in crystal topography

• Published in: Journal of molecular recognition Vol. 36; no. 9; pp. e3047 - n/a
• Main Authors: Chen, Shu‐wen W., Teulon, Jean‐Marie, Pellequer, Jean‐Luc
• Format: Journal Article
• Language: English
• Published: England Wiley Subscription Services, Inc 01.09.2023; Wiley
• Subjects: AFM; Atomic force microscopy; Biochemistry, Molecular Biology; Bti; Crystal growth; crystal protein; Crystallography; Crystals; high‐resolution imaging; insecticidal toxin; Life Sciences; L‐weight filter; Monomers; protoxin; Structural Biology; Structural members; Synergistic effect; Toxins; Weight; L-weight filter; high-resolution imaging; Bti; insecticidal toxin; AFM; crystal protein; protoxin
• ISSN: 0952-3499; 1099-1352
• DOI: 10.1002/jmr.3047

Cry11Aa and Cyt1Aa are two pesticidal toxins produced by Bacillus thuringiensis subsp. israelensis. To improve our understanding of the nature of their oligomers in the toxic actions and synergistic effects, we performed the atomic force microscopy to probe the surfaces of their natively grown crystals, and used the L‐weight filter to enhance the structural features. By L‐weight filtering, molecular sizes of the Cry11Aa and Cyt1Aa monomers obtained are in excellent agreement with the three‐dimensional structures determined by x‐ray crystallography. Moreover, our results show that the layered feature of a structural element distinguishes the topographic characteristics of Cry11Aa and Cyt1Aa crystals, suggesting that the Cry11Aa toxin has a better chance than Cyt1Aa for multimerization and therefore cooperativeness of the toxic actions.