Insecticidal toxins from Bacillus thuringiensis subsp. kenyae: gene cloning and characterization and comparison with B. thuringiensis subsp. kurstaki CryIA(c) toxins

Tersch, M A Von; Robbins, H L; Jany, C S; Johnson, Timothy B.

doi:10.1128/aem.57.2.349-358.1991

Cited by 25 publications

(5 citation statements)

References 39 publications

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“…Because of the demonstrated loss of measurable Cry proteins, and because it is possible that ELISA may detect the presence of inactivated Cry proteins, it is important to confirm the biological activity of the Cry proteins in an artificial diet assay using sensitive insects. In the present study, we were able to confirm the biological activity of Cry1Ab, Cry1Ac, Cry1F, and Cry2Aa in the artificial diet based on the known sensitivity of H. virescens neonates to those Cry proteins 33 – 35 . No clear biological activity was observed for Cry1B and Cry1C, but there is also no indication from the literature that those Cry proteins are active against H. virescens .…”

Section: Discussionsupporting

confidence: 68%

Effects of purified or plant-produced Cry proteins on Drosophila melanogaster (Diptera: Drosophilidae) larvae

Haller

Romeis

Meissle

2017

Sci Rep

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Although genetically engineered crops producing insecticidal Cry proteins from Bacillus thuringiensis (Bt) are grown worldwide, few studies cover effects of Bt crops or Cry proteins on dipteran species in an agricultural context. We tested the toxicity of six purified Cry proteins and of Bt cotton and Bt maize tissue on Drosophila melanogaster (Diptera: Drosophilidae) as a surrogate for decomposing Diptera. ELISA confirmed the presence of Cry proteins in plant material, artificial diet, and fly larvae, and concentrations were estimated. Median concentrations in emerging adult flies were below the limit of detection. Bioactivity of purified Cry proteins in the diet was confirmed by sensitive species assays using Heliothis virescens (Lepidoptera: Noctuidae). Purified Cry1Ab, Cry1Ac, Cry1B, Cry1C, Cry1F, or Cry2Aa, or leaf material from stacked Bt cotton (Bollgard II producing Cry1Ac and Cry2Ab) or Bt maize (SmartStax producing Cry1A.105, Cry1Fa2, Cry2Ab2, Cry3Bb1, Cry34Ab1 and Cry35Ab1) had no consistent effects on D. melanogaster survival, developmental time, adult body mass or morphometrics. However, D. melanogaster showed longer developmental time and smaller wing size when fed with cotton leaves from plants infested with H. virescens caterpillars compared to flies fed with leaves from uninfested plants, while no such effects were obvious for maize.

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Section: Discussionsupporting

confidence: 68%

Effects of purified or plant-produced Cry proteins on Drosophila melanogaster (Diptera: Drosophilidae) larvae

Haller

Romeis

Meissle

2017

Sci Rep

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“…Structural considerations (19,23) and experimental results obtained with other insects (24,25,34,50) suggest that the loop regions of domain II are involved in binding and specificity. Previously published results obtained with natural variants of Cry1Ac suggest that what is now considered loop 3 of domain II (19) affects toxicity to susceptible diamondback moth larvae (48). An inspection of alignments (Fig.…”

Section: Discussionmentioning

confidence: 90%

Cross-resistance of the diamondback moth indicates altered interactions with domain II of Bacillus thuringiensis toxins

Tabashnik

Malvar

Liu

et al. 1996

Appl Environ Microbiol

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We compared responses to six insecticidal crystal proteins from Bacillus thuringiensis by a Cry1A-resistant strain (NO-QA) and a susceptible strain (LAB-P) of the diamondback moth, Plutella xylostella. The resistant strain showed >100-fold cross-resistance to Cry1J and to H04, a hybrid with domains I and II of Cry1Ab and domain III of Cry1C. Cross-resistance was sixfold to Cry1Bb and threefold to Cry1D. The potency of Cry1I did not differ significantly between the resistant and susceptible strains. Cry2B did not kill resistant or susceptible larvae. By combining these new data with previously published results, we classified responses to 14 insecticidal crystal proteins by strains NO-QA and LAB-P. NO-QA showed high levels of resistance to Cry1Aa, Cry1Ab, and Cry1Ac and high levels of cross-resistance to Cry1F, Cry1J, and H04. Cross-resistance was low or nil to Cry1Ba, Cry1Bb, Cry1C, Cry1D, Cry1I, and Cry2A. Cry1E and Cry2B showed little or no toxicity to susceptible or resistant larvae. In dendrograms based on levels of amino acid sequence similarity among proteins, Cry1F and Cry1J clustered together with Cry1A proteins for domain II, but not for domain I or III. High levels of cross-resistance to Cry1Ab-Cry1C hybrid H04 show that although Cry1C is toxic to NO-QA, domain III of Cry1C is not sufficient to restore toxicity when it is combined with domains I and II of Cry1Ab. Thus, diamondback moth strain NO-QA cross-resistance extends beyond the Cry1A family of proteins to at least two other families that exhibit high levels of amino sequence similarity with Cry1A in domain II (Cry1F and Cry1J) and to a protein that is identical to Cry1Ab in domain II (H04). The results of this study imply that resistance to Cry1A alters interactions between the insect and domain II.

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“…This crystal protein shared 99·66% homology with the insecticidal toxin of Cry1A(c) from B. thuringiensis subsp. Kenyae (GenBank: ), which has been proven to have anti‐insect activity against Trichoplusia ni , Lymantria dispar , Heliothis zea and Heliothis virescens (Von Tersch et al. 1991).…”

Section: Resultsmentioning

confidence: 99%

The cry1Ac gene of Bacillus thuringiensis ZQ-89 encodes a toxin against long-horned beetle adult

Zhang

et al. 2011

Journal of Applied Microbiology

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Aims: Bacillus thuringiensis is toxic to many insects including Coleopteran pests. However, there is no report that B. thuringiensis is toxic to the adults of long‐horned beetle, Batocera horsfieldi, a pest of poplar trees. This work aims to select a B. thuringiensis strain toxic towards the adults of Asian long‐horned beetle. Methods and Results: A total of 504 B. thuringiensis strains were tested for the insecticidal activity to B. horsfieldi adults by artificial feeding. A strain of ZQ‐89 was found with a high toxicity to B. horsfieldi adults. The rectified lethal rate of ZQ‐89 to beetle was 55·33%. Additionally, the body weight and egg‐hatching rate of beetle, respectively, decreased by 2·22 and 19·62% after being fed with ZQ‐89. Further investigation found that the pure parasporal crystal had high toxicity to beetle adults. The ZQ‐89 crystal protein was purified and analysed by peptide‐mapping fingerprint and found it was highly homologous to Cry1Ac protein. The crystal protein gene was cloned and named cry1Ac89. The cry1Ac89 gene and its promoter were inserted into the plasmid pHT304 and then transformed into B. thuringiensis acrystalliferous strain BMB171. SDS‐PAGE analysis showed the BMB171‐Cry1Ac89 recombinant strain successfully expresses a 133‐kDa recombinant crystal protein with highly lethal activity to B. horsfieldi adults. Conclusions: The strain of ZQ‐89 is highly toxic to the adults of long‐horned beetle, and the crystal protein mainly contributes to the antipest role of this strain. The cry1Ac89 gene is a good candidate to be used for making transgenic trees or develop environment‐friendly bioinsecticides against long‐horned beetles such as B. horsfieldi in the future. Significance and Impact of the Study: It is the first report of a B. thuringiensis strain toxic to the adults of Asian long‐horned beetle, and the Cry1Ac protein is also firstly reported to be toxic to Coleopteran pests.

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Insecticidal toxins from Bacillus thuringiensis subsp. kenyae: gene cloning and characterization and comparison with B. thuringiensis subsp. kurstaki CryIA(c) toxins

Cited by 25 publications

References 39 publications

Effects of purified or plant-produced Cry proteins on Drosophila melanogaster (Diptera: Drosophilidae) larvae

Effects of purified or plant-produced Cry proteins on Drosophila melanogaster (Diptera: Drosophilidae) larvae

Cross-resistance of the diamondback moth indicates altered interactions with domain II of Bacillus thuringiensis toxins

The cry1Ac gene of Bacillus thuringiensis ZQ-89 encodes a toxin against long-horned beetle adult

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