ArticlePloS one2011
A soluble acetylcholinesterase provides chemical defense against xenobiotics in the pinewood nematode.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 64 citations in OpenAlex.
- Advances in Migratory Plant Endoparasitic Nematode Effectors.International journal of molecular sciences · 2024Review
- Phytochemical Analysis and Binding Interaction of Cotton Seed Cake Derived Compounds with Target Protein ofLife (Basel, Switzerland) · 2022Article
- Article
- FMRFamide-Like Peptide 22 Influences the Head Movement, Host Finding, and Infection ofFrontiers in plant science · 2021Article
- Differential expression of acetylcholinesterase 1 in response to various stress factors in honey bee workers.Scientific reports · 2019Article
- Laboratory bioassays on the response of honey bee (Apis mellifera L.) glutathione S-transferase and acetylcholinesterase to the oral exposure to copper, cadmium, and lead.Environmental science and pollution research international · 2019Article
- Article
- Caligus rogercresseyi acetylcholinesterase types and variants: a potential marker for organophosphate resistance.Parasites & vectors · 2018Article
- Expression of acetylcholinesterase 1 is associated with brood rearing status in the honey bee, Apis mellifera.Scientific reports · 2017Article
- Acetylcholinesterase secreted by Anisakis simplex larvae (Nematoda: Anisakidae) parasitizing herring, Clupea harengus: an inverse relationship of enzyme activity in the host-parasite system.Parasitology research · 2014Article
- Article
- Molecular and kinetic properties of two acetylcholinesterases from the western honey bee, Apis mellifera.PloS one · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pinewood nematode genome encodes at least three distinct acetylcholinesterases (AChEs). To understand physiological roles of the three pinewood nematode AChEs (BxACE-1, BxACE-2, and BxACE-3), BxACE-3 in particular, their tissue distribution and inhibition profiles were investigated. Immunohistochemistry revealed that BxACE-1 and BxACE-2 were distributed in neuronal tissues. In contrast, BxACE-3 was detected from some specific tissues and extracted without the aid of detergent, suggesting its soluble nature unlike BxACE-1 and BxACE-2. When present together, BxAChE3 significantly reduced the inhibition of BxACE-1 and BxACE-2 by cholinesterase inhibitors. Knockdown of BxACE-3 by RNA interference significantly increased the toxicity of three nematicidal compounds, supporting the protective role of BxACE-3 against chemicals. In summary, BxACE-3 appears to have a non-neuronal function of chemical defense whereas both BxACE-1 and BxACE-2 have classical neuronal function of synaptic transmission.
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