Midgut GPI-anchored proteins with alkaline phosphatase activity from the cotton boll weevil (Anthonomus grandis) are putative receptors for the Cry1B protein of Bacillus thuringiensis

Martins, E. S.; Monnerat, R. G.; Queiroz, Paulo Roberto Martins; Dumas, V. F.; Braz, Shélida Vasconcelos; Aguiar, Raimundo Wagner de Souza; Gomes, Ana C.; Sánchez, Jorge; Bravo, Alejandra; Ribeiro, Bergmann Morais

doi:10.1016/j.ibmb.2010.01.005

Cited by 42 publications

(31 citation statements)

References 71 publications

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“…In mosquito larvae, homologous APN, CAD-like, and alkaline phosphatase proteins have been described as Cry11 and Cry4 receptor proteins (6), and in Coleoptera a cadherin-like protein has been demonstrated to act as a Cry3Aa receptor (7). In coleopteran insects, other molecules, such as an ADAM-like metalloprotease (8) and alkaline phosphatase (9), have been proposed as putative Cry receptors. The best characterized Cry receptors, APN and CAD-like proteins, have been unequivocally involved in a Bt mode of action by gene silencing, resulting in a reduced sensitivity to toxin (10,11).…”

mentioning

confidence: 99%

Sodium Solute Symporter and Cadherin Proteins Act as Bacillus thuringiensis Cry3Ba Toxin Functional Receptors in Tribolium castaneum

Contreras

Schoppmeier

Real

et al. 2013

Journal of Biological Chemistry

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Background: Interaction with insect midgut receptors is required for Bacillus thuringienesis (Bt) toxicity. Results: RNAi knockdown of E-cadherin and sodium solute symporter (SSS) genes dramatically decreases Tribolium castaneum (Tc) larval susceptibility to Cry3Ba. A SSS fragment enhances Cry3Ba toxicity. Conclusion: E-cadherin and SSS but not aminopeptidase N are Cry3Ba receptors in Tc. Significance: For the first time, SSS was demonstrated as a Bt functional receptor.

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mentioning

confidence: 99%

Sodium Solute Symporter and Cadherin Proteins Act as Bacillus thuringiensis Cry3Ba Toxin Functional Receptors in Tribolium castaneum

Contreras

Schoppmeier

Real

et al. 2013

Journal of Biological Chemistry

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“…The strain that caused the highest mortality rate was B. thuringiensis kurstaki NRD-12 (Cry2A), with 64.48% of corrected mortality, followed by B. thuringiensis dendrolimus HD37 (Cry1Aa), with 61.98% (Table 3). Martins et al (25) analyzed 215 B. thuringiensis strains against the coleopteran Anthonomus grandis and found five strains that caused over 50% of mortality rate. Out of these five, the most toxic strain contained the cry1B gene and two cry2 genes.…”

Section: Resultsmentioning

confidence: 99%

“…Until then, works with Cry2 protein against coleopterans had still not been reported. Although Cry1 proteins have originally been related in regards to their toxicity for lepidopterans, many studies have already reported their toxicity for coleopterans (10, 23, 25, 26, 30). These results evidence the toxic potential of Cry1 and Cry2 proteins against coleopterans, which until then was essentially associated to Cry3 and Cry9 proteins (11, 19).…”

Section: Resultsmentioning

confidence: 99%

Bacillus thuringiensis monogenic strains: screening and interactions with insecticides used against rice pests

Pinto¹,

Dörr²,

Ribeiro³

et al. 2012

Braz. J. Microbiol.

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The screening of Bacillus thuringiensis (Bt) Cry proteins with high potential to control insect pests has been the goal of numerous research groups. In this study, we evaluated six monogenic Bt strains (Bt dendrolimus HD-37, Bt kurstaki HD-1, Bt kurstaki HD-73, Bt thuringiensis 4412, Bt kurstaki NRD-12 and Bt entomocidus 60.5, which codify the cry1Aa, cry1Ab, cry1Ac, cry1Ba, cry1C, cry2A genes respectively) as potential insecticides for the most important insect pests of irrigated rice: Spodoptera frugiperda, Diatraea saccharalis, Oryzophagus oryzae, Oebalus poecilus and Tibraca limbativentris. We also analyzed their compatibility with chemical insecticides (thiamethoxam, labdacyhalothrin, malathion and fipronil), which are extensively used in rice crops. The bioassay results showed that Bt thuringiensis 4412 and Bt entomocidus 60.5 were the most toxic for the lepidopterans, with a 93% and 82% mortality rate for S. frugiperda and D. saccharalis, respectively. For O. oryzae, the Bt kurstaki NRD-12 (64%) and Bt dendrolimus HD-37 (62%) strains were the most toxic. The Bt dendrolimus HD-37 strain also caused high mortality (82%) to O. poecilus, however the strains assessed to T. limbativentris caused a maximum rate of 5%. The assays for the Bt strains interaction with insecticides revealed the compatibility of the six strains with the four insecticides tested. The results from this study showed the high potential of cry1Aa and cry1Ba genes for genetic engineering of rice plants or the strains to biopesticide formulations.

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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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Midgut GPI-anchored proteins with alkaline phosphatase activity from the cotton boll weevil (Anthonomus grandis) are putative receptors for the Cry1B protein of Bacillus thuringiensis

Cited by 42 publications

References 71 publications

Sodium Solute Symporter and Cadherin Proteins Act as Bacillus thuringiensis Cry3Ba Toxin Functional Receptors in Tribolium castaneum

Sodium Solute Symporter and Cadherin Proteins Act as Bacillus thuringiensis Cry3Ba Toxin Functional Receptors in Tribolium castaneum

Bacillus thuringiensis monogenic strains: screening and interactions with insecticides used against rice pests

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

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