Receptors and Lethal Effect of<i>Bacillus thuringiensis</i>Insecticidal Crystal Proteins to the<i>Anticarsia gemmatalis</i>(Lepidoptera, Noctuidae)

Fiúza, Lidia Mariana; Knaak, Neiva; Silva, Rogerio Fernando Pires da; Henriques, João Antônio Pêgas

doi:10.1155/2013/940284

Cited by 12 publications

(11 citation statements)

References 55 publications

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“…On the other hand, it has been described that Cry2A was either nontoxic to A. gemmatalis (30) or toxic when tested by diet incorporation (31, 32). Our results support the high toxicity of Cry2Aa, especially for C.…”

Section: Discussionmentioning

confidence: 99%

Toxicity and Binding Studies of Bacillus thuringiensis Cry1Ac, Cry1F, Cry1C, and Cry2A Proteins in the Soybean Pests Anticarsia gemmatalis and Chrysodeixis (Pseudoplusia) includens

Bel

Sheets²,

Tan³

et al. 2017

Appl Environ Microbiol

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Anticarsia gemmatalis (velvetbean caterpillar) and Chrysodeixis includens (soybean looper, formerly named Pseudoplusia includens) are two important defoliating insects of soybeans. Both lepidopteran pests are controlled mainly with synthetic insecticides. Alternative control strategies, such as biopesticides based on the Bacillus thuringiensis (Bt) toxins or transgenic plants expressing Bt toxins, can be used and are increasingly being adopted. Studies on the insect susceptibilities and modes of action of the different Bt toxins are crucial to determine management strategies to control the pests and to delay outbreaks of insect resistance. In the present study, the susceptibilities of both soybean pests to the Bt toxins Cry1Ac, Cry1Fa, Cry1Ca, and Cry2Aa have been investigated. Bioassays performed in first-instar larvae showed that both insects are susceptible to all these toxins. Competition-binding studies carried out with Cry1Ac and Cry1Fa 125-iodine labeled proteins demonstrated the presence of specific binding sites for both of them on the midgut brush border membrane vesicles (BBMVs) of both A. gemmatalis and C. includens. Competition-binding experiments and specific-binding inhibition studies performed with selected sugars and lectins indicated that Cry1Ac and Cry1Fa share some, but not all, binding sites in the midguts of both insects. Also, the Cry1Ac- or Cry1Fa-binding sites were not shared with Cry1Ca or Cry2Aa in either soybean pest. This study contributes to the knowledge of Bt toxicity and midgut toxin binding sites in A. gemmatalis and C. includens and sheds light on the cross-resistance potential of Cry1Ac, Cry1Fa, Cry1Ca, and Cry2Aa Bt proteins as candidate proteins for Bt-pyramided crops.IMPORTANCE In the present study, the toxicity and the mode of action of the Bacillus thuringiensis (Bt) toxins Cry1Ac, Cry1Fa, Cry1Ca, and Cry2Aa in Anticarsia gemmatalis and Chrysodeixis includens (important defoliating pests of soybeans) have been investigated. These studies are crucial for determining management strategies for pest control. Bioassays showed that both insects were susceptible to the toxins. Competition-binding studies demonstrated the presence of Cry1Fa- and Cry1Ac-specific binding sites in the midguts of both pests. These results, together with the results from binding inhibition studies performed with sugars and lectins, indicated that Cry1Ac and Cry1Fa share some, but not all, binding sites, and that they were not shared with Cry1Ca or Cry2Aa in either soybean pest. This study contributes to the knowledge of Bt toxicity in A. gemmatalis and C. includens and sheds light on the cross-resistance potential of Cry1Ac, Cry1Fa, Cry1Ca, and Cry2Aa Bt proteins as candidate proteins for Bt-pyramided crops.

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Section: Discussionmentioning

confidence: 99%

Toxicity and Binding Studies of Bacillus thuringiensis Cry1Ac, Cry1F, Cry1C, and Cry2A Proteins in the Soybean Pests Anticarsia gemmatalis and Chrysodeixis (Pseudoplusia) includens

Bel

Sheets²,

Tan³

et al. 2017

Appl Environ Microbiol

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“…The effects of several Cry toxins have been previously demonstrated in larvae of A. gemmatalis (Bel et al, ; Mushtaq et al, , ; Fiuza et al, ). The mode of action and toxicity of some different Cry toxins were recently described by Mushtaq et al () and indicated that the domain III of Cry1Ac, which has a lectin fold, is not important for toxicity.…”

Section: Resultsmentioning

confidence: 90%

“…In Brazil, transgenic soybean expressing Cry1Ac (one type of Bt toxin) has been commercialized since 2013 (Bel, Sheets, Tan, Narvac, & Escriche, ). The effect of Cry toxins against A. gemmatalis has been previously described, but its receptor still remains unidentified (Fiuza, Knaak, Fernando, Antônio, & Henriques, ). Some recent works demonstrated the susceptibility of A. gemmatalis larvae to several Cry toxins, and Cry1Ac was pointed as the most successful (Bel et al, ; Mushtaq et al, ; Mushtaq, Shakoori, & Jurat‐Fuentes, ).…”

Section: Introductionmentioning

confidence: 99%

Biochemical characterization of digestive membrane‐associated alkaline phosphatase from the velvet bean caterpillar Anticarsia gemmatalis

Silva

Ramos

Seckler

et al. 2019

Arch Insect Biochem Physiol

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In Brazil, the use of transgenic plants expressing the insecttoxic Bacillus thuringiensis endotoxin has been successfully used as pest control management since 2013 in transgenic soybean lineages against pest caterpillars such as Helicoverpa armigera. These toxins, endogenously expressed by the plants or sprayed over the crops, are ingested by the insect and bind to receptors in the midgut of these animals, resulting in disruption of digestion and lower insect survival rates. Here, we identified and characterized a membraneassociated alkaline phosphatase (ALP) in the midgut of Anticarsia gemmatalis, the main soybean defoliator pest in Brazil, and data suggested that it binds to Cry1Ac toxin in vitro. Our data showed a peak of ALP activity in homogenate samples of the midgut dissected from the 4th and 5th instars larvae. The brush border membrane vesicles obtained from the midgut of these larvae were used to purify a 60 kDa ALP, as detected by in-gel activity and in vitro biochemical characterization using pharmacological inhibitors and mass spectrometry. When Cry1Ac toxin was supplied to the diet, it was efficient in decreasing larval weight gain and survival. Indeed, in vitro incubation of Cry1Ac toxin with the purified ALP resulted in a 43% decrease in ALP specific activity and enzyme-linked immunosorbent assay showed that ALP interacts with Cry1Ac toxin in vitro, thus suggesting that ALP could function as a Cry toxin ligand. This is a first report characterizing an ALP in A. gemmatalis.

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“…Cry2Aa is toxic to the velvetbean caterpillar A. gemmatalis, but not toxic to S. frugiperda [44]. However, Fiuza et al (2013) report that Cry2Aa is not toxic to A. gemmatalis [45]. Cry2Aa is less toxic (LC 50 = 4.30 µg/g) to H. virescens and H. armigera than Cry1Ac (LC 50 = 0.73 µg/g) with lethal dose ratios of 5.89 and 6.54 of LC 50 , respectively [46,47].…”

Section: Discussionmentioning

confidence: 99%

Insecticidal Activity of 11 Bt toxins and 3 Transgenic Maize Events Expressing Vip3Aa19 to Black Cutworm, Agrotis ipsilon (Hufnagel)

Yan

Ren

et al. 2020

Insects

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Black cutworm (BCW), Agrotis ipsilon (Hufnagel), is an occasional pest of maize that can cause considerable economic loss and injury to corn seedlings. This research mainly assessed the susceptibility of BCW neonates to 11 Bt toxins (Cry1Ab, Cry1Ac, Cry1Ah, Cry1F, Cry1Ie, Cry1B, Cry2Aa, Vip3_ch1, Vip3_ch4, Vip3Ca2, Vip3Aa19) by exposing neonates to an artificial diet containing Bt toxins and evaluated the efficacy of three transgenic maize events (C008, C009, C010) expressing Vip3Aa19 toxin against BCW. The toxin-diet bioassay data indicated that Vip3Aa19 protein (LC50 = 0.43 μg/g) was the most active against BCW. Chimeric protein Vip3_ch1 (LC50 = 5.53 μg/g), Cry1F (LC50 = 83.62 μg/g) and Cry1Ac (LC50 = 184.77 μg/g) were less toxic. BCW was very tolerant to the other Bt toxins tested, with LC50 values more than 200 μg/g. Greenhouse studies were conducted with artificial infestations at the whorl stage by placing second-instar BCW larvae into whorl leaf and the fourth-instar larvae at the base of maize seedings. These results suggest that these transgenic maize events expressing Vip3Aa19 can provide effective control for BCW.

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Receptors and Lethal Effect ofBacillus thuringiensisInsecticidal Crystal Proteins to theAnticarsia gemmatalis(Lepidoptera, Noctuidae)

Cited by 12 publications

References 55 publications

Toxicity and Binding Studies of Bacillus thuringiensis Cry1Ac, Cry1F, Cry1C, and Cry2A Proteins in the Soybean Pests Anticarsia gemmatalis and Chrysodeixis (Pseudoplusia) includens

Toxicity and Binding Studies of Bacillus thuringiensis Cry1Ac, Cry1F, Cry1C, and Cry2A Proteins in the Soybean Pests Anticarsia gemmatalis and Chrysodeixis (Pseudoplusia) includens

Biochemical characterization of digestive membrane‐associated alkaline phosphatase from the velvet bean caterpillar Anticarsia gemmatalis

Insecticidal Activity of 11 Bt toxins and 3 Transgenic Maize Events Expressing Vip3Aa19 to Black Cutworm, Agrotis ipsilon (Hufnagel)

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