Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)

Bergamasco, V. B.; Mendes, Déborah; Fernandes, Odair Aparecido; Desidério, Janete Apparecida; Lemos, Manoel Victor Franco

doi:10.1016/j.jip.2012.11.011

Cited by 82 publications

(57 citation statements)

References 51 publications

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“…Synergism has been observed between the Vip3Aa and Cyt2Aa proteins against Chilo suppressalis (Lepidoptera: Crambidae) and S. exigua after their coexpression in Escherichia coli; contrarily, this protein combination was slightly antagonistic against C. quinquefasciatus (66). Bergamasco et al (74) reported synergism between Vip3A and Cry1Ia in three Spodoptera species (S. frugiperda, S. albula, and S. cosmioides [Lepidoptera: Noctuidae]) but slight antagonism in Spodoptera eridania (Lepidoptera: Noctuidae). Antagonism between the Vip3A and Cry1A or Cry1Ca proteins in H. virescens was described (75): antagonism was found for the combination of Cry1Ca and Vip3Aa, Vip3Ae, or Vip3Af and for the combination of Vip3Af and either Cry1Aa or Cry1Ac.…”

Section: Insecticidal Activitymentioning

confidence: 99%

“…10). Specific binding to brush border membrane vesicles (BBMVs) prepared from susceptible insects was first shown by using biotin-labeled Vip3Aa and Vip3Af (68,69,74,87,92,93,95). Interestingly, Vip3Aa also binds specifically to BBMVs of the nonsusceptible insect O. nubilalis (87), which indicates that specific binding is not sufficient to produce toxicity.…”

Section: Mode Of Actionmentioning

confidence: 99%

“…In Prays oleae (Lepidoptera: Yponomeutidae) and Agrotis segetum (Lepidoptera: Noctuidae), Vip3Aa bound to a 65-kDa protein, while Cry1Ac bound to a 210-kDa band in P. oleae and to a 120-kDa band in A. segetum (69,97). In S. littoralis, Vip3Aa bound proteins of 55 and 100 kDa (68), and in Ephestia kuehniella (Lepidoptera: Pyralidae), S. frugiperda, S. albula, S. cosmioides, and S. eridania, Vip3Aa bound to a protein of 65 kDa (74,88), to which Cry1Ia also bound in the four Spodoptera species (74).…”

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

254

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: Mode Of Actionmentioning

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

254

261

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“…Moreover, a strong synergistic interaction was found between these two factors towards D. pini, indicating that formulations containing both proteins can be effective in combating this dangerous pest of conifers. Several authors have also observed synergisms and high insecticidal activity of Vip and crystal toxin mixtures against different lepidopteran pests: Anticarsia gemmatalis, Chrysodeixis includes (Crialesi- , S. albula, S. cosmoides, S. frugiperda (Bergamasco et al 2013), S. exigua, C. suppressalis (Yu et al 2012) and Diatraea saccharalis . However, the authors have also noticed antagonistic Cry/Vip interactions in other insects.…”

Section: Discussionmentioning

confidence: 98%

Interaction between toxin crystals and vegetative insecticidal proteins of Bacillus thuringiensis in lepidopteran larvae

2017

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Insecticides based on crystalline toxins of Bacillus thuringiensis are very good biological plant protection products. However, the spectrum of activity of some toxins is narrow or resistance among insects has been developed. We tested the insecticidal activity of crystals of the B. thuringiensis MPU B9 strain alone and supplemented with Vip3Aa proteins against important pests: Spodoptera exigua Hübner (Lepidoptera: Noctuidae), Cydia pomonella L. (Lepidoptera: Tortricidae) and Dendrolimus pini L. (Lepidoptera: Lasiocampidae). The Cry toxins were more active for D. pini but less active against S. exigua and C. pomonella than Vip3Aa. Supplementation of Cry toxins by small amounts of vegetative insecticidal proteins demonstrated synergistic effect and significantly enhanced the toxicity of the insecticide. The results indicate the utility of Cry and Vip3Aa toxins mixtures to control populations of crops and forests insect pests.

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“…Metarhizium anisopliae is also known as an entomopathogenic fungus and is applied to control insect pests; Metarhizium anisopliae-extracted toxin, destruxin, is lethal to insects (Sharif, 2010;Smagghe et al, 2013). Bacillus thuringiensis is a widely represented entomopathogenic bacterium that produce crystal (Cry) toxins 1, 2, 4, 10, and 11 and is used as the first choice effective biological control against many kinds of insects from the orders Coleoptera, Lepidoptera, and Diptera (Ben-Dov, 2014;Bergamasco et al, 2013). we assumed that it originated from coconut palm rhinoceros beetle O. rhinoceros (Lee et al, 2015).…”

mentioning

confidence: 99%

Simultaneous detection of fungal, bacterial, and viral pathogens in insects by multiplex PCR and capillary electrophoresis

Kwak¹,

Nam²,

Choi³

et al. 2015

International Journal of Industrial Entomology

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Beetles Protaetia brevitarsis seulensis Kolbe (Coleoptera: Cetoniidae) and Allomyrina dichotoma Linn. (Coleoptera: Scarabaeidae) are widely used in traditional medicine, and the number of insect-rearing farms is increasing in South Korea. The purpose of this study was to establish a multiplex PCR-based assay for rapid simultaneous detection of multiple pathogens causing insect diseases. Six insect parasites such as fungi Beauveria bassiana (Bals.-Criv.) Vuill. (Hypocreales: Cordycipitaceae) and Metarhizium anisopliae (Metschn.) Sorokin (Hypocreales: Clavicipitaceae), bacteria Bacillus thuringiensis Berliner (Bacillales: Bacillaceae), Pseudomonas aeruginosa Migula (Pseudomonadales: Pseudomonadaceae), and Serratia marcescens Bizio (Enterobacteriales: Enterobacteriaceae), and Oryctes rhinoceros nudivirus were chosen based on the severity and incidence rate of insect diseases in South Korea. Pathogen-specific primers were designed and successfully applied for simultaneous detection of multiple infectious agents in farm-bred insects P. b. seulensis and A. dichotoma using multiplex PCR and high resolution capillary electrophoresis. Our results indicate that multiplex PCR is an effective and time-saving method for simultaneous detection of multiple infections in insects, and the QIAxcel capillary electrophoresis system is useful for quantitative evaluation of the individual impact of each infectious agent on the severity of insect disease. The approach designed in this study can be utilized for rapid and accurate diagnostics of infection in insect farms.© 2015 The Korean Society of Sericultural Sciences Int. J. Indust. Entomol. 30(2), 64-74 (2015) IntroductionFollowing a global trend of using natural products from insects, the Korean government has been encouraging the development of insect resources for environmental and dietary purposes, traditional medicine, and as pets (Kim et al., 2013 Vol. 30, No. (1), pp. 64-74 (2015) Pseudomonas aeruginosa is reported as a virulent bacterial pathogen not only for insects but also for mammals (Jander et al., 2000), where it causes infection of the respiratory tract, especially in cystic fibrosis patients (Spiker et al., 2004). Similar to Pseudomonas aeruginosa, Serratia marcescens is known as an opportunistic bacterium (El-Aasar et al., 2013); it is also used to control apple maggot fly population and as a source of insecticidal agents such as toxin luxA (Hejazi and Falkiner, 1997; Lauzon et al., 2003). Oryctes rhinoceros virus Rhabdionvirus oryctes Hüger was first discovered in oil palms in Malaysia 40 years ago and is currently used for the control of rhinoceros beetle population in Malaysia (Huger, 2005;Ramle et al., 2005).We have identified this virus in an A. dichotoma-breeding farm in 2014 in Korea (Lee, 2015).Extensive large-scale insect breeding has resulted in frequent occurrence of insect infection due to multiple pathogens. Here, we developed a multiplex PCR-based approach that allowed simultaneous detection of six insect pathogens using specific primer se...

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Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)

Cited by 82 publications

References 51 publications

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Interaction between toxin crystals and vegetative insecticidal proteins of Bacillus thuringiensis in lepidopteran larvae

Simultaneous detection of fungal, bacterial, and viral pathogens in insects by multiplex PCR and capillary electrophoresis

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