Analysis of Cry8Ka5-binding proteins from Anthonomus grandis (Coleoptera: Curculionidae) midgut

Nakasu, Erich Yukio Tempel; Firmino, Alexandre Augusto Pereira; Dias, Simoni Campos; Rocha, T. L.; Ramos, H. B.; Oliveira, Gustavo R.; Lucena, Wagner Alexandre; Carlini, Célia R.; Grossi-de-Sá, Maria Fátima

doi:10.1016/j.jip.2010.01.012

Cited by 20 publications

(18 citation statements)

References 22 publications

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“…Cry8Ka toxins have been reported to be toxic to the cotton boll weevil, A. grandis (Coleoptera: Curculionidae) [Nakasu et al, 2010]. Therefore, we included this insect species in the bioassays to determine the toxicity of the three Cry8 proteins found in INTA Fr7-4.…”

Section: Insect Bioassays Of Wild-type and Recombinant Cry8 Proteinsmentioning

confidence: 99%

Sequence and Expression of Two cry8 Genes from Bacillus thuringiensis INTA Fr7-4, a Native Strain from Argentina

Navas

Berretta²,

Pérez³

et al. 2014

Microb Physiol

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We found and characterized two cry8 genes from the Bacillus thuringiensis strain INTA Fr7-4 isolated in Argentina. These genes, cry8Kb3 and cry8Pa3, are located in a tandem array within a 13,200-bp DNA segment sequenced from a preparation of total DNA. They encode 1,169- and 1,176-amino-acid proteins, respectively. Both genes were cloned with their promoter sequences and the proteins were expressed separately in an acrystalliferous strain of B. thuringiensis leading to the formation of ovoid crystals in the recombinant strains. The toxicity against larvae of Anthonomus grandis Bh. (Coleoptera: Curculionidae) of a spore-crystal suspension from the recombinant strain containing cry8Pa3 was similar to that of the parent strain INTA Fr7-4.

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Section: Insect Bioassays Of Wild-type and Recombinant Cry8 Proteinsmentioning

confidence: 99%

Sequence and Expression of Two cry8 Genes from Bacillus thuringiensis INTA Fr7-4, a Native Strain from Argentina

Navas

Berretta²,

Pérez³

et al. 2014

Microb Physiol

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“…Cry proteins have multiple binding determinants, possibly specified independently by domains II and III. Moreover, Cry toxins interact with other classes of proteins in the Coleoptera order, such as ALP (molecular weight ~65 kDa), V-ATPase and the Heat-Shock Cognate protein (~ 80 kDa) and the ADAM metalloprotease (~30 kDa) (Hua et al 2001;Ochoa-Campuzano et al 2007;Martins et al 2010;Nakasu et al 2010). Any signals in the ligand blot for Cry1B and Cry3A would be related with these proteic groups.…”

Section: The Modes Of Action Of Cry Toxins In Coleopterans: the Case mentioning

confidence: 99%

Biological Activity of Insecticidal Toxins: Structural Basis, Site-Directed Mutagenesis and Perspectives

López-Pazos¹,

Cerón²

2013

Genetic Manipulation of DNA and Protein - Examples From Current Research

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“…V‐ATPases are located in the goblet cell apical membrane, which is involved in energy production and conversion (Nishi and Forgac, ; Beyenbach and Wieczorek, ). Evidence from a number of studies appears to indicate a role for V‐ATPase in the toxicity of Cry proteins in susceptible insects (Krishnamoorthy et al ., ; Chen et al ., ; Nakasu et al ., ; Contreras et al ., ; Xu et al ., ; Zhou et al ., ). The potential role of the V‐ATPase subunit A in mediating the toxicity of Bt Cry toxins in C. suppressalis has not previously been examined.…”

Section: Introductionmentioning

confidence: 99%

The midgut V‐ATPase subunit A gene is associated with toxicity to crystal 2Aa and crystal 1Ca‐expressing transgenic rice in Chilo suppressalis

Qiu

Sun

Jiang

et al. 2019

Insect Molecular Biology

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Insecticidal crystal (Cry) proteins produced by the bacterium Bacillus thuringiensis (Bt) are toxic to a diverse range of insects. Transgenic rice expressing Cry1A, Cry2A and Cry1C toxins have been developed that are lethal to Chilo suppressalis, a devastating insect pest of rice in China. Identifying the mechanisms underlying the interactions of Cry toxins with susceptible hosts will improve both our understanding of Cry protein toxicology and long‐term efficacy of Bt crops. In this study, we tested the hypothesis that V‐ATPase subunit A contributes to the action of Cry1Ab/1Ac, Cry2Aa and Cry1Ca toxins in C. suppressalis. The full‐length V‐ATPase subunit A transcript was initially cloned from the C. suppressalis larval midgut and then used to generate double‐stranded RNA (dsRNA)‐producing bacteria. Toxicity assays using transgenic rice lines TT51 (Cry1Ab and Cry1Ac fusion genes), T2A‐1 (Cry2Aa), and T1C‐19 (Cry1Ca) in conjunction with V‐ATPase subunit A dsRNA‐treated C. suppressalis larvae revealed significantly reduced larval susceptibility to T2A‐1 and T1C‐19 transgenic rice, but not to TT51 rice. These results suggest that the V‐ATPase subunit A plays a crucial role in mediating Cry2Aa and Cry1Ca toxicity in C. suppressalis. These findings will have significant implications on the development of future resistance management tools.

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Analysis of Cry8Ka5-binding proteins from Anthonomus grandis (Coleoptera: Curculionidae) midgut

Cited by 20 publications

References 22 publications

Sequence and Expression of Two <b><i>cry8</i></b> Genes from <b><i>Bacillus thuringiensis</i></b> INTA Fr7-4, a Native Strain from Argentina

Sequence and Expression of Two <b><i>cry8</i></b> Genes from <b><i>Bacillus thuringiensis</i></b> INTA Fr7-4, a Native Strain from Argentina

Biological Activity of Insecticidal Toxins: Structural Basis, Site-Directed Mutagenesis and Perspectives

The midgut V‐ATPase subunit A gene is associated with toxicity to crystal 2Aa and crystal 1Ca‐expressing transgenic rice in Chilo suppressalis

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