Expression of Bacillus thuringiensis Toxins in Insect Cells

2017 ◽  
pp. 99-110 ◽  
Author(s):  
Bergmann Morais Ribeiro ◽  
Érica Soares Martins ◽  
Raimundo Wagner de Souza Aguiar ◽  
Roberto Franco Teixeira Corrêa
Keyword(s):  
Bacillus Thuringiensis ◽  
Insect Cells

scholarly journals Bacillus thuringiensisCry1Da_7 and Cry1B.868 Protein Interactions with Novel Receptors Allow Control of Resistant Fall Armyworms,Spodoptera frugiperda(J.E. Smith)

2019 ◽  
Vol 85 (16) ◽  
Author(s):  
Yanfei Wang ◽  
Jinling Wang ◽  
Xiaoran Fu ◽  
Jeffrey R. Nageotte ◽  
Jennifer Silverman ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Protein Interactions ◽  
Spodoptera Frugiperda ◽  
Insect Cells ◽  
Fall Armyworm ◽  
Insecticidal Protein ◽  
Row Crops ◽  
Content Type ◽  
Resistance Risk ◽  
Important Pest

ABSTRACTTwo new modifiedBacillus thuringiensis(Bt) proteins, Cry1Da_7 and Cry1B.868, with activity against fall armyworms (FAW),Spodoptera frugiperda(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 availableBtproteins 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.IMPORTANCEThere 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),Spodoptera frugiperda, a maize pest that already has developed resistance toBacillus thuringiensis(Bt) 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 availableBtproteins 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.

CHARACTERIZATION OF CULTURED INSECT CELLS SELECTED BY BACILLUS THURINGIENSIS CRYSTAL TOXIN

2004 ◽  
Vol 40 (10) ◽  
pp. 312 ◽  
Author(s):  
KAIYU LIU ◽  
BINGLIAN ZHENG ◽  
HUAZHU HONG ◽  
CAIFU JIANG ◽  
RONG PENG ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Insect Cells ◽  
Crystal Toxin

scholarly journals Cry2A toxins from Bacillus thuringiensis expressed in insect cells are toxic to two lepidopteran insects

2008 ◽  
Vol 24 (12) ◽  
pp. 2941-2948 ◽  
Author(s):  
G. M. S. Lima ◽  
R. W. S. Aguiar ◽  
R. F. T. Corrêa ◽  
E. S. Martins ◽  
A. C. M. Gomes ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Insect Cells ◽  
Lepidopteran Insects

Parasporal crystals produced by oligosporogenous mutants of Bacillus thuringiensis (Spo− Cr+)

1980 ◽  
Vol 26 (4) ◽  
pp. 486-491 ◽  
Author(s):  
Donovan E. Johnson ◽  
Debra M. Niezgodski ◽  
George M. Twaddle
Keyword(s):  
Bacillus Thuringiensis ◽  
Inclusion Bodies ◽  
Insect Cells ◽  
Crystalline Inclusion ◽  
Wild Type ◽  
In Vitro Technique ◽  
Mutant Strains ◽  
Embedded Particles ◽  
Parasporal Crystals

Six oligosporogenic (Spo−) mutant strains of Bacillus thuringiensis were selected from survivors of treatment with N-methyl-N′-nitro-N-nitrosoguanidine. Each strain was blocked at or before stage II of spore development, but all produced typical bipyramidal-shaped crystalline inclusion bodies. Toxicity of the parasporal endotoxin isolated from the mutant strains was assayed by an in vitro technique using cultured insect cells, and was comparable with that of normal wild-type parasporal protein. Multiple parasporal inclusion bodies per cell were often produced, and smaller embedded particles were numerous and distinct.

Structural implications for the transformation of the Bacillus thuringiensis δ-endotoxins from water-soluble to membrane-inserted forms

2001 ◽  
Vol 29 (4) ◽  
pp. 571-577 ◽  
Author(s):  
J. Li ◽  
D. J. Derbyshire ◽  
B. Promdonkoy ◽  
D. J. Ellar
Keyword(s):  
Bacillus Thuringiensis ◽  
Conformational Change ◽  
Conformational Changes ◽  
Large Scale ◽  
Insect Cells ◽  
Water Soluble ◽  
Single Amino Acid ◽  
The Core ◽  
High Affinity Site ◽  
Temperature Factors

Crystal structures combined with biochemical data show that the δ-endotoxins from Bacillus thuringiensis are structurally poised towards large-scale, irreversible conformational changes that transform them from the soluble protein bound at the cell surface into a membrane-embedded form causing lysis of susceptible insect cells. Cry δ-endotoxins are made of a helix bundle, a β-prism and a β-sandwich. The conformational change involves an umbrella-like opening between the helix-4,5-hairpin and the remaining helices, and between the helical domain and the two sheet domains. Comparison of Cry1Ac structures with and without the bound receptor ligand GalNAc associates occupation of the high-affinity site on the β-sandwich with an increase of temperature factors in the helical, pore-forming domain, which may indicate how receptor binding could trigger the required major conformational change. The structure of Cyt δ-endotoxins indicates that the surface helix hairpins must peel away to expose the β-strands for membrane attack. Single amino acid substitutions in hinge residues or the core can restore activity following an inhibitory mutation.

Bacillus thuringiensis enzyme-digested delta endotoxin: effect on cultured insect cells

Science ◽  
1976 ◽  
Vol 194 (4268) ◽  
pp. 954-956 ◽  
Author(s):  
D. Murphy ◽  
S. Sohi ◽  
P. Fast
Keyword(s):  
Bacillus Thuringiensis ◽  
Insect Cells ◽  
Delta Endotoxin
Sign in / Sign up

Export Citation Format

Share Document