Susceptibility of Spodoptera frugiperda and S. exigua to Bacillus thuringiensis Vip3Aa insecticidal protein

Chakroun, Maissa; Bel, Yolanda; Caccia, Silvia; Abdelkefi-Mesrati, Lobna; Escriche, Baltasar; Ferré, Juan

doi:10.1016/j.jip.2012.03.021

Cited by 73 publications

(78 citation statements)

References 29 publications

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“…With Vip3 proteins, depending on the Vip3 protein and the insect species being considered, it is not uncommon to find that while mortality is reached with a high concentration of Vip3 protein, strong growth inhibition (or even complete growth arrest) is observed with lower concentrations (16,62,(67)(68)(69). Therefore, "functional mortality" (dead insects plus those remaining at larval instar L1) better represents the effectiveness of the Vip3 protein in these cases (16,70,71). Table 2 summarizes the results that have been reported on the insecticidal activity of proteins of the Vip3Aa subfamily.…”

Section: Insecticidal Activitymentioning

confidence: 99%

“…Only the values for the protoxin form are given, since there are no reports indicating relevant differences in the insecticidal activities of the protoxin and the activated forms (16), with the exceptions of the activities of Vip3Aa16 against S. exigua and Vip3Af1 against Spodoptera frugiperda (Lepidoptera: Noctuidae) (71,72). Despite the very small differences among Vip3Aa sequences, some proteins may exhibit significant differences in toxicity to the same insect species (16,59,73).…”

Section: Insecticidal Activitymentioning

confidence: 99%

“…Although an early study claimed that the minimal fragment that retained insecticidal activity after proteolysis was the 33-kDa fragment (57), all subsequent studies are in favor of the 62-to 66-kDa fragment being the Vip3Aa toxic core (58,60,68,69,71,72,(87)(88)(89)(92)(93)(94). Interestingly, the 20-kDa fragment produced upon proteolytic processing of the Vip3Aa16 protoxin copurifies with the 62-kDa fragment, suggesting that after activation of the full-length protein, the two fragments remain together (89).…”

Section: Mode Of Actionmentioning

confidence: 99%

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Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

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243

261

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SUMMARYEntomopathogenic bacteria produce insecticidal proteins that accumulate in inclusion bodies or parasporal crystals (such as the Cry and Cyt proteins) as well as insecticidal proteins that are secreted into the culture medium. Among the latter are the Vip proteins, which are divided into four families according to their amino acid identity. The Vip1 and Vip2 proteins act as binary toxins and are toxic to some members of the Coleoptera and Hemiptera. The Vip1 component is thought to bind to receptors in the membrane of the insect midgut, and the Vip2 component enters the cell, where it displays its ADP-ribosyltransferase activity against actin, preventing microfilament formation. Vip3 has no sequence similarity to Vip1 or Vip2 and is toxic to a wide variety of members of the Lepidoptera. Its mode of action has been shown to resemble that of the Cry proteins in terms of proteolytic activation, binding to the midgut epithelial membrane, and pore formation, although Vip3A proteins do not share binding sites with Cry proteins. The latter property makes them good candidates to be combined with Cry proteins in transgenic plants (Bacillus thuringiensis-treated crops [Bt crops]) to prevent or delay insect resistance and to broaden the insecticidal spectrum. There are commercially grown varieties of Bt cotton and Bt maize that express the Vip3Aa protein in combination with Cry proteins. For the most recently reported Vip4 family, no target insects have been found yet.

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Section: Insecticidal Activitymentioning

confidence: 99%

Section: Insecticidal Activitymentioning

confidence: 99%

Section: Mode Of Actionmentioning

confidence: 99%

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Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

Self Cite

243

261

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“…Bacillus thuringiensis (Bt) é uma bactéria Gram-positiva, com atividade inseticida a diversas pragas agrícolas, que pode ser encontrada naturalmente no solo, superfície de plantas, em insetos mortos e em grãos armazenados (Bravo et al, 1998). Em razão de sua atividade entomopatogênica, essa bactéria é amplamente empregada no controle biológico de insetos-praga e pode ser utilizada na forma de bioinseticidas ou em plantas geneticamente modificadas.…”

Section: Introductionunclassified

“…Herrero et al (2004). Para a expressão das proteínas Vip3A, utilizou-se a metodologia descrita por Chakroun et al (2012), que altera a concentração de isopropil-D-tiogalactopiranosídeo (IPTG) para 1 mmol L -1 na indução da expressão. As proteínas foram recuperadas por centrifugação, em tampão fosfato 20 mmol L -1 (NaH 2 PO 4 .H 2 O e Na 2 HPO 4 .2H 2 O) pH 7,4, com 0,5 mol L -1 NaCl.…”

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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Impact of Spodoptera frugiperda neonate pretreatment conditions on Vip3Aa19 insecticidal protein activity and laboratory bioassay variation

Silva

Spencer

Camargo

et al. 2015

Pest Management Science

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BACKGROUNDVariation in response to insecticidal proteins is common upon repetition of insect bioassays. Understanding this variation is a prerequisite to detecting biologically important differences. We tracked neonate Spodoptera frugiperda (J.E. Smith) susceptibility to Vip3Aa19 over 17 generations using standardized bioassay methods. Five larval pretreatment conditions and one bioassay condition were tested to determine whether susceptibility was affected. These included: storage time; prefeeding; storage at reduced temperature; storage at reduced humidity; colony introgression of field‐collected individuals. Extremes of photoperiod during the bioassay itself were also examined.RESULTS LC50 values for two strains of S. frugiperda varied 6.6‐fold or 8.8‐fold over 17 generations. Storage time and humidity had no impact on Vip3Aa19 susceptibility, whereas prefeeding significantly reduced subsequent mortality (by 27%). Storage at reduced temperature increased mortality for one colony (from 45.6 to 73.0%) but not for the other. Introgression of field‐collected individuals affected susceptibility at the first generation but not for subsequent generations. A 24 h bioassay photophase significantly reduced susceptibility (by 26%) for both colonies.CONCLUSIONCertain pretreatment and bioassay conditions were identified that can affect S. frugiperda Vip3Aa19 susceptibility, but innate larval heterogeneity was also present. Our observations should help to increase the consistency of insecticidal protein bioassay results. © 2015 Syngenta Crop Protection, LLC. Pest Management Science published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

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Susceptibility of Spodoptera frugiperda and S. exigua to Bacillus thuringiensis Vip3Aa insecticidal protein

Cited by 73 publications

References 29 publications

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

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

Impact of Spodoptera frugiperda neonate pretreatment conditions on Vip3Aa19 insecticidal protein activity and laboratory bioassay variation

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