A New Plant Insecticide for control of the European Corn Borer12

Pepper, Bailey P.; Carruth, Lauren

doi:10.1093/jee/38.1.59

Cited by 36 publications

(26 citation statements)

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“…The RyR has been investigated extensively in mammals, and it has been proved that there are three RyR isoforms encoded by three different genes on different chromosomes in mammals 17–22. Although the ryanodine receptor of insects has been used as a target of insecticide for more than six decades,23, 24 very little was known about it until Takeshima and colleagues first described it in D. melanogaster in 1994 25. Recently, Puente et al 26 reported that the H. virescens RyR C‐terminal amino acid sequence shares 74% identity with D. melanogaster and 47.9–50.1% identity with vertebrate isoforms.…”

Section: Discussionmentioning

confidence: 99%

Cloning, characterisation and expression profiling of the cDNA encoding the ryanodine receptor in diamondback moth, Plutella xylostella (L.) (Lepidoptera: Plutellidae)

Guo

Tang

Dong

et al. 2012

Pest Management Science

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Section: Discussionmentioning

confidence: 99%

Cloning, characterisation and expression profiling of the cDNA encoding the ryanodine receptor in diamondback moth, Plutella xylostella (L.) (Lepidoptera: Plutellidae)

Guo

Tang

Dong

et al. 2012

Pest Management Science

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“…The ground stem wood of the shrub Ryania speciosa, a native plant of tropical America has been used as an insecticide (Heal 1949;Pepper and Carruth 1945). The main alkaloid in such extracts, ryanodine ( Fig.…”

Section: Ryanodine and Ryanoids-insecticides Based On A Natural Productmentioning

confidence: 99%

“…Radiolabeled ryanodine ([3H]ryanodine) has been used to purify RyRs from a variety of tissues. Ryanodine itself has long been utilized as an insecticide (Pepper and Carruth 1945), but its mammalian toxicity has precluded its continued use. Synthetic derivatives of the Ryania alkaloids have been explored and extensive structure-activity studies pursued (Lehmberg and Casida 1994;Waterhouse et al 1987).…”

Section: Introductionmentioning

confidence: 99%

Insect ryanodine receptors: molecular targets for novel pest control chemicals

2008

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Ryanodine receptors (RyRs) are a distinct class of ligand-gated calcium channels controlling the release of calcium from intracellular stores. They are located on the sarcoplasmic reticulum of muscle and the endoplasmic reticulum of neurons and many other cell types. Ryanodine, a plant alkaloid and an important ligand used to characterize and purify the receptor, has served as a natural botanical insecticide, but attempts to generate synthetic commercial analogues of ryanodine have proved unsuccessful. Recently two classes of synthetic chemicals have emerged resulting in commercial insecticides that target insect RyRs. The phthalic acid diamide class has yielded flubendiamide, the first synthetic ryanodine receptor insecticide to be commercialized. Shortly after the discovery of the phthalic diamides, the anthranilic diamides were discovered. This class has produced the insecticides Rynaxypyr and Cyazypyr. Here we review the structure and functions of insect RyRs and address the modes of action of phthalic acid diamides and anthranilic diamides on insect ryanodine receptors. Particularly intersting is the inherent selectivity both chemical classes exhibit for insect RyRs over their mammalian counterparts. The future prospects for RyRs as a commercially-validated target site for insect control chemicals are also considered.

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“…We created a structural model of DBM RyR in the ryanodine‐bound state based on the rabbit RyR1 structure bound with ryanodine (PDB ID 5TAW). Ryanodine is the first generation of insecticide used to target insect RyRs . Despite extensive efforts in search of a safe derivative, no selective analogue has ever been identified.…”

Section: Resultsmentioning

confidence: 99%

Homology modeling and docking study of diamondback moth ryanodine receptor reveals the mechanisms for channel activation, insecticide binding and resistance

Lin

Hao

Cao

et al. 2019

Pest Management Science

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BACKGROUND Diamide insecticides, including phthalic and anthranilic diamides, target insect ryanodine receptors (RyRs) and cause misregulation of calcium signaling in insect muscles and neurons. Several resistance mutations have been reported to reduce the efficacy of the diamides, but the exact binding sites and mechanism of resistance mutations are not clear. RESULTS The recent breakthrough in structural studies of mammalian RyRs has deepened our understanding of these giant calcium‐release channels, but structural information about insect RyRs is still scarce. The only reported high‐resolution structure is from the N‐terminal domain of diamondback moth (DBM) RyR determined by our group. Here, we generate several homology models of full‐length DBM RyR representing different functional states and dock the diamide insecticides into the structural models using Schrodinger software. These models reveal the specific structural features, activation mechanism, structural difference between functional states, ligand‐binding sites and insecticide‐binding sites of DBM RyR. By comparing the structures of wild‐type and insecticide‐resistant mutants, we propose a model depicting how the mutations affect the insecticide binding. We also identify the key difference between mammalian and insect RyRs that may explain the species‐specific binding properties of diamides. CONCLUSION The binding sites for three activators Ca2+, ATP and caffeine, and regulator ryanodine are conserved in insect and mammalian RyRs, but the binding site for diamide insecticides is species‐specific. The phthalic and anthranilic diamides have distinct binding properties in DBM, which can be interfered by resistance mutations located in the transmembrane region. © 2019 Society of Chemical Industry

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A New Plant Insecticide for control of the European Corn Borer12

Cited by 36 publications

References 0 publications

Cloning, characterisation and expression profiling of the cDNA encoding the ryanodine receptor in diamondback moth, Plutella xylostella (L.) (Lepidoptera: Plutellidae)

Cloning, characterisation and expression profiling of the cDNA encoding the ryanodine receptor in diamondback moth, Plutella xylostella (L.) (Lepidoptera: Plutellidae)

Insect ryanodine receptors: molecular targets for novel pest control chemicals

Homology modeling and docking study of diamondback moth ryanodine receptor reveals the mechanisms for channel activation, insecticide binding and resistance

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