Acetylcholine Receptors: Purification, Structure and Interaction with Insecticides

Eldefrawi, Amira T.; Eldefrawi, Mohyee E.; Mansour, Nabil

doi:10.1007/978-1-4615-8834-4_4

Cited by 2 publications

(2 citation statements)

References 37 publications

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“…Additionally, it has been shown that this group of mutations coexists as a resistant haplotype; when T197I was produced in Xenopus oocytes, either alone or in combination, it effectively inhibited permethrin sensitivity. The T917I amino acid change is relevant to pyrethroid resistance via the kdr-type nerve insensitivity mechanism and can be employed as a molecular marker for resistance detection [45].…”

Section: Head Licementioning

confidence: 99%

Perspective Chapter: Genomics, Proteomics, and System Biology of Insecticides Resistance in Insects

Manzoor Malik,

Fazal,

Khatoon

et al. 2023

Insecticides - Advances in Insect Control and Sustainable Pest Management

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Insecticide resistance is an inherited change in pest population exposure to a specific insecticide or group of insecticides. Overuse, misuse, and high interbreeding rates have led to insecticide resistance. Genomic technologies reveal mechanisms of resistance, including decreased target-site sensitivity and increased detoxification. Genomic projects have cloned and identified targeted genes in Drosophila melanogaster and studied resistance-associated mutations in various pest insects. Advancements in genome sequencing and annotation techniques have explored complex multigene enzyme systems, such as glutathione-S-transferases, esterases, and cytochrome P450, which facilitate insecticide resistance. Identifying specific genes involved in resistance and targeted genes is essential for developing new insecticides and strategies to control pests. Insects with resistance metabolize insecticidal compounds faster due to increased catalytic rate and gene amplification. So, system biology plays a very important role in the insect resistance against insecticides and different chemicals such as DDT and permethrin. From system biology, not only the identification of genes was done, but also the protein-protein interactions were found out, which were responsible in the insect resistance.

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Section: Head Licementioning

confidence: 99%

Perspective Chapter: Genomics, Proteomics, and System Biology of Insecticides Resistance in Insects

Manzoor Malik,

Fazal,

Khatoon

et al. 2023

Insecticides - Advances in Insect Control and Sustainable Pest Management

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“…In another study, no difference in the ability of antisera to precipitate receptor or toxin-receptor complexes was observed [4]. The reported inhibition of [12' I] a-BuTx binding to membrane-associated AcChR has varied from 0% to 100% [4][5][6][7][8], while reports of inhibition of toxin binding t o detergent-solubilized AcChR have varied from 50% to 100% [5,7,9,101. Similar variability (20-100%) has been reported for inhibition of [ HI -acetylcholine binding to membrane-associated and detergent-solubilized AcChR [8, 111.…”

mentioning

confidence: 94%

Inhibition of α‐bungarotoxin binding to acetylcholine receptors by antisera from animals with experimental autoimmune myasthenia gravis

Claudio

Raftery

1980

J Supramol Struct

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Conditions are described for an assay that allows the percent inhibition of alpha-bungarotoxin binding to acetylcholine receptors by antisera and monovalent antigen-binding fragments of antibody molecules (Fab) to be determined. Anti-Torpedo californica acetylcholine-receptor antisera, prepared in New Zealand White rabbits and Lewis rats, were tested for the ability to inhibit [125I]-alpha-bungarotoxin binding to membrane-associated and detergent-solubilized T californica acetylcholine receptors. Similar inhibition studies were performed using rabbit antisera and antigen-binding fragments prepared against each of the four acetylcholine receptor subunits. Antisera and antigen-binding fragments prepared against intact receptor could inhibit a maximum of 50% of the alpha-bungarotoxin binding to solubilized receptor. The results using monovalent antigen-binding fragments indicated that the inhibition was not due to antibody-mediated aggregation of receptor molecules. Rabbits and rats immunized with receptor denatured by sodium dodecyl sulfate all produced antisera that could bind to nondenatured receptor, but none of these animals developed experimental autoimmune myasthenia gravis. These results suggest that the antigenic determinants present on acetylcholine receptors responsible for induction of experimental autoimmune myasthenia gravis are lost with sodium dodecyl sulfate denaturation. A strong correlation was also observed between the presence of experimental autoimmune myasthenia gravis in rats and rabbits and the ability of the antisera from these animals to inhibit 50% of alpha-bungarotoxin binding to solubilized acetylcholine receptors.

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Acetylcholine Receptors: Purification, Structure and Interaction with Insecticides

Cited by 2 publications

References 37 publications

Perspective Chapter: Genomics, Proteomics, and System Biology of Insecticides Resistance in Insects

Perspective Chapter: Genomics, Proteomics, and System Biology of Insecticides Resistance in Insects

Inhibition of α‐bungarotoxin binding to acetylcholine receptors by antisera from animals with experimental autoimmune myasthenia gravis

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