Isolation and characterization of acetylcholinesterase from Drosophila.

Gnagey, A.L.; Forte, Michael; Rosenberry, Terrone L.

doi:10.1016/s0021-9258(18)45200-3

Cited by 185 publications

(33 citation statements)

References 61 publications

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“…Interactions of potential inhibitors with the amino acid residues Trp71, Trp83, Tyr370, Phe371 and His480 of acetylcholinesterase are similar to those reported in the literature (Fournier et al, 1993;Gnagey et al, 1987). The best evaluated inhibitors in binding a nity parameters were Aspergillol B and Aspernolide A, considering that the interactions were similar to those observed in controls I40 and pyriproxyfen for Tyr71, Trp83, Tyr370 and Tyr374 residues, contributing to the increase in binding a nity.…”

Section: Molecular Docking Simulations and Biological Activitysupporting

confidence: 80%

Larvicidal and Oviposition Activity of Against Vector Aedes Aegypti and Molecular Docking Studies of Metabolites from the Crude Extract of the Endophytic Fungus Aspergillus Sp. Isolated from Bertholletia Excelsa Humn. & Bonpl.

Araújo

Marinho

Sena

et al. 2021

Preprint

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This work showed the crude extract of the endophytic fungus Aspergillus sp, isolated from the almonds of Bertholletia excelsa Humn & Bonlp collected in the Brazilian Amazon, oviposition deterrent, and larvicidal activity of against Aedes aegypti. In the oviposition deterrence test was observed that females able to lay eggs preferred the control oviposition sites (46.6%), suggesting the extract also could repel the oviposition. Futhermore, the extract showed larvicidal activity with LC50 26.86 µg/mL at 24 hours and 18.75 µg/mL at 48 hours. Molecular docking studies were carried out to elucidate the mechanism of action of the compounds identified against the enzyme acetylcholinesterase. The compound Aspergillol B was a potent larvicide with potential for inhibition for the acetylcholinesterase enzyme (-7.74 Kcal/mol). These unprecedented results reported indicate that the secondary metabolites obtained from crude extract of Aspergillus sp. present useful biological potential against vectors of public health importance and antibiotic-resistant bacteria.

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Section: Molecular Docking Simulations and Biological Activitysupporting

confidence: 80%

Larvicidal and Oviposition Activity of Against Vector Aedes Aegypti and Molecular Docking Studies of Metabolites from the Crude Extract of the Endophytic Fungus Aspergillus Sp. Isolated from Bertholletia Excelsa Humn. & Bonpl.

Araújo

Marinho

Sena

et al. 2021

Preprint

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“…Interestingly, F290 is present and F288 is absent in both sequences, a property of all invertebrate AChE sequences, explaining a wider substrate specificity than vertebrate AChE (Vellom et al 1993). Examination of the C-terminal ends of the deduced amino acid sequences showed, in all available dipteran AChEs, a hydrophobic peptide compatible with a signal for glycolipid addition, indicating that a portion of the C-terminus is cleaved posttranslationally and replaced by a glycolipid anchor, as in Drosophila and several species of mosquitoes (Gnagey et al 1987;Bourguet et al 1996Bourguet et al , 1997. It is also observed, in all cases, that a free cysteine is present in the C-terminus upstream of the putative cleavage site of the hydrophobic peptide (not shown in figure 1).…”

Section: (A) Two Ace Genes In Anopheles Gambiaementioning

confidence: 97%

A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non–homologous to theacegeneDrosophila

Weill

Fort

Berthomieu

et al. 2002

Proc. R. Soc. Lond. B

253

234

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Acetylcholinesterase (AChE) is the target of two major insecticide families, organophosphates (OPs) and carbamates. AChE insensitivity is a frequent resistance mechanism in insects and responsible mutations in the ace gene were identified in two Diptera, Drosophila melanogaster and Musca domestica. However, for other insects, the ace gene cloned by homology with Drosophila does not code for the insensitive AChE in resistant individuals, indicating the existence of a second ace locus. We identified two AChE loci in the genome of Anopheles gambiae, one (ace-1) being a new locus and the other (ace-2) being homologous to the gene previously described in Drosophila. The gene ace-1 has no obvious homologue in the Drosophila genome and was found in 15 mosquito species investigated. In An. gambiae, ace-1 and ace-2 display 53% similarity at the amino acid level and an overall phylogeny indicates that they probably diverged before the differentiation of insects. Thus, both genes are likely to be present in the majority of insects and the absence of ace-1 in Drosophila is probably due to a secondary loss. In one mosquito (Culex pipiens), ace-1 was found to be tightly linked with insecticide resistance and probably encodes the AChE OP target. These results have important implications for the design of new insecticides, as the target AChE is thus encoded by distinct genes in different insect groups, even within the Diptera: ace-2 in at least the Drosophilidae and Muscidae and ace-1 in at least the Culicidae. Evolutionary scenarios leading to such a peculiar situation are discussed.

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“…The presence of AChE has been demonstrated in a variety of animal tissues and enzymes from a number of different sources, including fish electric organs, mammalian erythrocyte, insect and mammalian brain, and other tissues. These enzymes have been purified and characterized (4)(5)(6)(7)(8). AChE is virtually a ubiquitous enzyme in vertebrates and invertebrates, and in mammals, it is localized in certain areas of the central nervous system and in organs and glands that are controlled by the parasympathetic division of the autonomic nervous system.…”

Section: Acetylcholinesterasementioning

confidence: 99%

Mechanism of action of organophosphorus and carbamate insecticides.

Fukuto

1990

Environ Health Perspect

780

281

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Organophosphorus and carbamate insecticides are toxic to insects and mammals by virtue of their ability to inactivate the enzyme acetylcholinesterase. This review addresses the mechanism of inhibition of acetylcholinesterase by organophosphorus and carbamate esters, focusing on structural requirements necessary for anticholinesterase activity. The inhibition of acetylcholinesterase by these compounds is discussed in terms of reactivity and steric effects. The role of metabolic activation or degradation in the overall intoxication process is also discussed.

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Isolation and characterization of acetylcholinesterase from Drosophila.

Cited by 185 publications

References 61 publications

Larvicidal and Oviposition Activity of Against Vector Aedes Aegypti and Molecular Docking Studies of Metabolites from the Crude Extract of the Endophytic Fungus Aspergillus Sp. Isolated from Bertholletia Excelsa Humn. & Bonpl.

Larvicidal and Oviposition Activity of Against Vector Aedes Aegypti and Molecular Docking Studies of Metabolites from the Crude Extract of the Endophytic Fungus Aspergillus Sp. Isolated from Bertholletia Excelsa Humn. & Bonpl.

A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non–homologous to theacegeneDrosophila

Mechanism of action of organophosphorus and carbamate insecticides.

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Isolation and characterization of acetylcholinesterase from Drosophila.

Cited by 185 publications

References 61 publications

Larvicidal and Oviposition Activity of Against Vector Aedes Aegypti and Molecular Docking Studies of Metabolites from the Crude Extract of the Endophytic Fungus Aspergillus Sp. Isolated from Bertholletia Excelsa Humn. &amp; Bonpl.

Larvicidal and Oviposition Activity of Against Vector Aedes Aegypti and Molecular Docking Studies of Metabolites from the Crude Extract of the Endophytic Fungus Aspergillus Sp. Isolated from Bertholletia Excelsa Humn. &amp; Bonpl.

A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non–homologous to theacegeneDrosophila

Mechanism of action of organophosphorus and carbamate insecticides.

Contact Info

Product

Resources

About

Larvicidal and Oviposition Activity of Against Vector Aedes Aegypti and Molecular Docking Studies of Metabolites from the Crude Extract of the Endophytic Fungus Aspergillus Sp. Isolated from Bertholletia Excelsa Humn. & Bonpl.

Larvicidal and Oviposition Activity of Against Vector Aedes Aegypti and Molecular Docking Studies of Metabolites from the Crude Extract of the Endophytic Fungus Aspergillus Sp. Isolated from Bertholletia Excelsa Humn. & Bonpl.