Biochemistry and Genetics of Insect Resistance to <i>Bacillus thuringiensis</i>

Ferré, Juan; Rie, Jeroen Van

doi:10.1146/annurev.ento.47.091201.145234

Cited by 790 publications

(577 citation statements)

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“…Although no study was conducted to clarify the mechanisms of resistance to Cry1F protein of S. frugiperda, the midgut binding site (including cadherin, alkaline phosphatase and aminopeptidases N) modification to Cry proteins were the most probable mechanism (Ferré and Van Rie 2002, Jurat-Fuentes et al 2011, Tiewsiri and Wang 2011 that would not substantially alter the other characters of the resistant strain. Our previous studies had shown that Cry1F-resistant S. frugiperda were not affected by Cry1F when they fed on Cry1F maize, even though they contained a high dose of bioactive Cry1F protein (Tian et al 2012(Tian et al , 2013.…”

Section: Parametersmentioning

confidence: 99%

Eliminating host-mediated effects demonstrates Bt maize producing Cry1F has no adverse effects on the parasitoid Cotesia marginiventris

et al. 2013

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The fall armyworm, Spodoptera frugiperda ( J. E. Smith) (Lepidoptera: Noctuidae), is an important pest of maize in the United States and many tropical areas in the western hemisphere. In 2001, Herculex I® (Cry1F) maize was commercially planted in the United States to control Lepidoptera, including S. frugiperda. In 2006, a population of S. frugiperda was discovered in Puerto Rico that had evolved resistance to Cry1F maize in the field, making it the first well-documented case of an insect with field resistance to a plant producing protein from Bacillus thuringiensis (Bt). Using this resistant population, we conducted tri-trophic studies with a natural enemy of S. frugiperda. By using resistantS. frugiperda, we were able to overcome possible prey-mediated effects and avoid concerns about potential differences in laboratory-or field-derived Bt resistance. We used the Cry1F-resistant S. frugiperda to evaluate effects of Cry1F on Cotesia marginiventris (Cresson) (Hymenoptera: Braconidae), a larval endoparasitoid of S. frugiperda, over five generations. Our results clearly demonstrate that Cry1F maize does not affect development, parasitism, survivorship, sex ratio, longevity or fecundity of C. marginiventris when they parasitize Cry1F maize-fed S. frugiperda.Furthermore, the level of Cry1F protein in the leaves was strongly diluted when transferred from Bt maize to S. frugiperda and was not detected in larvae, cocoons or adults of C. marginiventris. Our results refute previous reports of C. marginiventris being harmed by Bt proteins and suggest that such results were caused by prey-mediated effects due to using Bt-susceptible lepidopteran hosts. RightsWorks produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted. Abstract The fall armyworm, Spodoptera frugiperda (J. E. Smith) (Lepidoptera: Noctuidae), is an important pest of maize in the United States and many tropical areas in the western hemisphere. In 2001, Herculex I Ò (Cry1F) maize was commercially planted in the United States to control Lepidoptera, including S. frugiperda. In 2006, a population of S. frugiperda was discovered in Puerto Rico that had evolved resistance to Cry1F maize in the field, making it the first well-documented case of an insect with field resistance to a plant producing protein from Bacillus thuringiensis (Bt). Using this resistant population, we conducted tri-trophic studies with a natural enemy of S. frugiperda. By using resistant S. frugiperda, we were able to overcome possible prey-mediated effects and avoid concerns about potential differences in laboratory-or field-derived Bt resistance. We used the Cry1F-resistant S. frugiperda to evaluate effects of Cry1F on Cotesia marginiventris (Cresson) (Hymenoptera: Braconidae), a larval endoparasitoid of S. frugiperda, over five generations. Our results clearly demonstrate that Cry1F maize does not affect development, parasitism, survivorship, sex ratio, longevity or fecundity ...

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Section: Parametersmentioning

confidence: 99%

Eliminating host-mediated effects demonstrates Bt maize producing Cry1F has no adverse effects on the parasitoid Cotesia marginiventris

et al. 2013

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“…Entretanto, apesar das vantagens, atualmente há grande preocupação com o uso generalizado de culturas Bt, uma vez que elas podem acelerar a seleção de organismos resistentes (Zhang et al, 2013), quando estratégias de manejo adequadas, como adoção de áreas de refúgio, não são utilizadas. O surgimento da resistência pode estar relacionado à ligação das proteínas inseticidas a receptores no intestino médio das lagartas (Ferré & Van Rie, 2002). Alternativas para retardar a evolução da resistência têm sido bastante estudadas e misturas de toxinas têm sido consideradas mais eficazes se utilizadas antes da evolução da resistência, mesmo sob pressão de seleção contínua (Xue et al, 2005;Bergamasco et al, 2013).…”

Section: Introductionunclassified

Interação de proteínas Cry1 e Vip3A de Bacillus thuringiensis para controle de lepidópteros-praga

Crialesi-Legori

Davolos

Lemes

et al. 2014

Pesq. agropec. bras.

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Resumo -O objetivo deste trabalho foi avaliar a suscetibilidade das lagartas Anticarsia gemmatalis (Lepidoptera: Erebidae) e Chrysodeixis includens (Lepidoptera: Noctuidae) às proteínas Cry1 e Vip3A, bem como determinar se há a interação entre essas proteínas no controle das duas espécies. Bioensaios com as proteínas isoladas e em combinações foram realizados, e as concentrações letais CL 50 e CL 90 foram estimadas para cada condição. As proteínas Cry1Aa, Cry1Ac e Vip3Af foram as mais efetivas no controle de A. gemmatalis, enquanto Cry1Ac, Vip3Aa e Vip3Af foram mais efetivas no de C. includens. As proteínas Cry1Ac e Cry1Ca causaram maior inibição do desenvolvimento das larvas sobreviventes à CL 50 , em ambas as espécies. Combinações entre Vip3A e Cry1 apresentam efeito sinérgico no controle das espécies e a combinação Vip3Aa+Cry1Ea destaca-se no controle de A. gemmatalis e C. includens. Essas proteínas combinadas são promissoras na construção de plantas piramidadas, para o controle simultâneo das pragas.Termos para indexação: Anticarsia gemmatalis, Chrysodeixis includens, manejo da resistência, piramidação de genes, sinergismo, soja transgênica. Interaction of Cry1 and Vip3A proteins of Bacillus thuringiensis for the control of lepidopteran insect pestsAbstract -The objective of this work was to evaluate the susceptibility of Anticarsia gemmatalis (Lepidoptera: Erebidae) and Chrysodeixis includens (Lepidoptera: Noctuidae) caterpillars to Cry1 and Vip3A proteins, as well as to determine if there is any interaction between these proteins on the control of the two species. Bioassays with both isolated and combined proteins were carried out, and lethal concentrations LC 50 and LC 90 were estimated for each condition. Cry1Aa, Cry1Ac, and Vip3Af were the more effective proteins for the control of A. gemmatalis, while Cry1Ac, Vip3Aa, and Vip3Af were more effective for the control of C. includens. Cry1Ac and Cry1Ca proteins caused the highest inhibition to the development of larvae that survived the LC 50 dose in both species. Different combinations of Vip3A and Cry1 have synergistic effect in the control of both species, and the combination Vip3Aa + Cry1Ea showed an outstanding control of A. gemmatalis and C. includens. These proteins are promising for building pyramided plants for the simultaneous control of the pests.

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“…In developing these markers an understanding of how resistance to the Bt toxins arises is paramount. In the majority of Cry-resistant insect species investigated, resistance has been linked to an alteration in the binding of Bt toxins to midgut epithelia, often correlated with reduced expression of a protein ligand (reviewed by Ferré and Van Rie, 2002). In H. armigera, Cry1Ac resistance was linked to an alteration in Cry1Ac binding to a cadherin-like protein (Akhurst et al, 2003;Xu and Wu, 2008).…”

Section: Introductionmentioning

confidence: 99%

Diversity of aminopeptidases, derived from four lepidopteran gene duplications, and polycalins expressed in the midgut of Helicoverpa armigera: Identification of proteins binding the δ-endotoxin, Cry1Ac of Bacillus thuringiensis

Angelucci

Barrett-Wilt²,

Hunt

et al. 2008

Insect Biochemistry and Molecular Biology

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Helicoverpa armigera midgut proteins that bind the Bacillus thuringiensis (Bt) δ-endotoxin Cry1Ac were purified by affinity chromatography. SDS-PAGE showed that several proteins were eluted with N-acetylgalactosamine and no further proteins were detected after elution with urea. Tandem mass spectral data for tryptic peptides initially indicated that the proteins resembled aminopeptidases (APNs) from other lepidopterans and cDNA sequences for seven APNs were isolated from H. armigera through a combination of cloning with primers derived from predicted peptide sequences and established EST libraries. Phylogenetic analysis showed lepidopteran APN genes in nine clades of which five were part of a lepidopteran-specific radiation. The Cry1Ac-binding proteins were then identified with four of the seven HaAPN genes. Three of those four APNs are likely orthologs of APNs characterised as Cry1Ac-binding proteins in other lepidopterans. The fourth Cry1Ac-binding APN has orthologs not previously identified as Cry1Ac-binding partners. The HaAPN genes were expressed predominantly in the midgut through larval development. Each showed consistent expression along the length of the midgut but five of the genes were expressed at levels about two orders of magnitude greater than the remaining two. The remaining mass spectral data identified sequences encoding polycalin proteins with multiple lipocalin-like domains. A polycalin has only been previously reported in another lepidopteran, Bombyx mori, but polycalins in both species are now linked with binding of Bt Cry toxins. This is the first report of hybrid, lipocalin-like domains in shorter polycalin sequences that are not present in the longest sequence. We propose that these hybrid domains are generated by alternative splicing of the mRNA.

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Biochemistry and Genetics of Insect Resistance to Bacillus thuringiensis

Cited by 790 publications

References 128 publications

Eliminating host-mediated effects demonstrates Bt maize producing Cry1F has no adverse effects on the parasitoid Cotesia marginiventris

Eliminating host-mediated effects demonstrates Bt maize producing Cry1F has no adverse effects on the parasitoid Cotesia marginiventris

Interação de proteínas Cry1 e Vip3A de Bacillus thuringiensis para controle de lepidópteros-praga

Diversity of aminopeptidases, derived from four lepidopteran gene duplications, and polycalins expressed in the midgut of Helicoverpa armigera: Identification of proteins binding the δ-endotoxin, Cry1Ac of Bacillus thuringiensis

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