6WPC

Crystal structure of Bacillus thuringiensis Cry1A.2 tryptic core variant

Summary for 6WPC

• Entry DOI: 10.2210/pdb6wpc/pdb
• Descriptor: Cry1A.2 (2 entities in total)
• Functional Keywords: bacillus thuringiensis, b.t., toxin, 3-domain cry
• Biological source: Bacillus thuringiensis
• Total number of polymer chains: 4
• Total formula weight: 265349.44

Authors

Rydel, T.J.,Evdokimov, A. (deposition date: 2020-04-27, release date: 2021-03-17, Last modification date: 2023-10-18)

Primary citation

Chen, D.,Moar, W.J.,Jerga, A.,Gowda, A.,Milligan, J.S.,Bretsynder, E.C.,Rydel, T.J.,Baum, J.A.,Semeao, A.,Fu, X.,Guzov, V.,Gabbert, K.,Head, G.P.,Haas, J.A.
Bacillus thuringiensis chimeric proteins Cry1A.2 and Cry1B.2 to control soybean lepidopteran pests: New domain combinations enhance insecticidal spectrum of activity and novel receptor contributions.
Plos One, 16:e0249150-e0249150, 2021

PubMed Abstract: Two new chimeric Bacillus thuringiensis (Bt) proteins, Cry1A.2 and Cry1B.2, were constructed using specific domains, which provide insecticidal activity against key lepidopteran soybean pests while minimizing receptor overlaps between themselves, current, and soon to be commercialized plant incorporated protectants (PIP's) in soybean. Results from insect diet bioassays demonstrate that the recombinant Cry1A.2 and Cry1B.2 are toxic to soybean looper (SBL) Chrysodeixis includens Walker, velvetbean caterpillar (VBC) Anticarsia gemmatalis Hubner, southern armyworm (SAW) Spodoptera eridania, and black armyworm (BLAW) Spodoptera cosmioides with LC50 values < 3,448 ng/cm2. Cry1B.2 is of moderate activity with significant mortality and stunting at > 3,448 ng/cm2, while Cry1A.2 lacks toxicity against old-world bollworm (OWB) Helicoverpa armigera. Results from disabled insecticidal protein (DIP) bioassays suggest that receptor utilization of Cry1A.2 and Cry1B.2 proteins are distinct from each other and from current, and yet to be commercially available, Bt proteins in soy such as Cry1Ac, Cry1A.105, Cry1F.842, Cry2Ab2 and Vip3A. However, as Cry1A.2 contains a domain common to at least one commercial soybean Bt protein, resistance to this common domain in a current commercial soybean Bt protein could possibly confer at least partial cross resistance to Cry1A2. Therefore, Cry1A.2 and Cry1B.2 should provide two new tools for controlling many of the major soybean insect pests described above.

PubMed: 34138865
DOI: 10.1371/journal.pone.0249150

Experimental method

X-RAY DIFFRACTION (2.99 Å)