6OVB

Crystal structure of a Bacillus thuringiensis Cry1Da tryptic core variant

Summary for 6OVB

• Entry DOI: 10.2210/pdb6ovb/pdb
• Descriptor: Active core crystal toxin protein 1D (2 entities in total)
• Functional Keywords: bacillus thuringiensis, cry toxin, b.t., toxin
• Biological source: Bacillus thuringiensis
• Total number of polymer chains: 1
• Total formula weight: 64964.96

Authors

Rydel, T.J.,Halls, C.,Evdokimov, A.G.,Beishir, S.C. (deposition date: 2019-05-07, release date: 2019-06-19, Last modification date: 2023-10-11)

Primary citation

Wang, Y.,Wang, J.,Fu, X.,Nageotte, J.R.,Silverman, J.,Bretsnyder, E.C.,Chen, D.,Rydel, T.J.,Bean, G.J.,Li, K.S.,Kraft, E.,Gowda, A.,Nance, A.,Moore, R.G.,Pleau, M.J.,Milligan, J.S.,Anderson, H.M.,Asiimwe, P.,Evans, A.,Moar, W.J.,Martinelli, S.,Head, G.P.,Haas, J.A.,Baum, J.A.,Yang, F.,Kerns, D.L.,Jerga, A.
Bacillus thuringiensis Cry1Da_7 and Cry1B.868 Protein Interactions with Novel Receptors Allow Control of Resistant Fall Armyworms, Spodoptera frugiperda (J.E. Smith).
Appl.Environ.Microbiol., 85:-, 2019

PubMed Abstract: Two new modified () proteins, Cry1Da_7 and Cry1B.868, with activity against fall armyworms (FAW), (J.E. Smith), were evaluated for their potential to bind new insect receptors compared to proteins currently deployed as plant-incorporated protectants (PIPs) in row crops. Results from resistant insect bioassays, disabled insecticidal protein (DIP) bioassays, and cell-based assays using insect cells expressing individual receptors demonstrate that receptor utilizations of the newly modified Cry1Da_7 and Cry1B.868 proteins are distinct from each other and from those of commercially available proteins such as Cry1F, Cry1A.105, Cry2Ab, and Vip3A. Accordingly, these two proteins target different insect proteins in FAW midgut cells and when pyramided together should provide durability in the field against this economically important pest. There is increased concern with the development of resistance to insecticidal proteins currently expressed in crop plants, especially against high-resistance-risk pests such as fall armyworm (FAW), , a maize pest that already has developed resistance to () proteins such as Cry1F. Lepidopteran-specific proteins that bind new insect receptors will be critical in managing current Cry1F-resistant FAW and delaying future resistance development. Results from resistant insect assays, disabled insecticidal protein (DIP) bioassays, and cell-based assays using insect cells expressing individual receptors demonstrate that target receptors of the Cry1Da_7 and Cry1B.868 proteins are different from each other and from those of commercially available proteins such as Cry1F, Cry1A.105, Cry2Ab, and Vip3A. Therefore, pyramiding these two new proteins in maize will provide durable control of this economically important pest in production agriculture.

PubMed: 31175187
DOI: 10.1128/AEM.00579-19

Experimental method

X-RAY DIFFRACTION (2.611 Å)