In Silico Study of the Resistance to Organophosphorus Pesticides Associated with Point Mutations in Acetylcholinesterase of Lepidoptera: B. mandarina, B. mori, C. auricilius, C. suppressalis, C. pomonella, H. armígera, P. xylostella, S. frugiperda, and S. litura

Abstract

An in silico analysis of the interaction between the complex-ligands of nine acetylcholinesterase (AChE) structures of Lepidopteran organisms and 43 organophosphorus (OPs) pesticides with previous resistance reports was carried out. To predict the potential resistance by structural modifications in Lepidoptera insects, due to proposed point mutations in AChE, a broad analysis was performed using computational tools, such as homology modeling and molecular docking. Two relevant findings were revealed: (1) Docking results give a configuration of the most probable spatial orientation of two interacting molecules (AChE enzyme and OP pesticide) and (2) a predicted ΔGb. The mutations evaluated in the form 1 acetylcholinesterase (AChE-1) and form 2 acetylcholinesterase (AChE-2) structures of enzymes do not affect in any way (there is no regularity of change or significant deviations) the values of the binding energy (ΔGb) recorded in the AChE–OPs complexes. However, the mutations analyzed in AChE are associated with a structural modification that causes an inadequate interaction to complete the phosphorylation of the enzyme.

Predicting the insecticide-driven mutations in a crop pest insect: Evidence for multiple polymorphisms of acetylcholinesterase gene with potential relevance for resistance to chemicals

“…These results suggest that mutations may have little effects on the protein-pesticide interaction. They may rather induce inadequate steric interaction that prevents the completion of the phosphorylation of the enzyme, as formerly proposed by Reyes-Espinosa et al (2019). This assumption was further confirmed by calculations of pKa values of the active site of the wild-type and mutant AChE1 of B. tabaci, and evidenced the alteration of the AChE1-Acetylcholine interaction induced by the mutation F392W.…”

Status of Acetylcholinesterase Mediated Organophosphate Resistance in Cattle Tick, Rhipicephalus Microplus (Acari: Ixodidae)

“…The site near triad His ( F331W, F331F/C); near anionic site (I129V/ T); acyl pocket (F290Y) and near oxyanion hole (A201S) mutations were associated with target site resistance in various insects and mites [67]. Recent a molecular models of AChE-1 were generated to know the modified enzyme by resistance-associated mutations in lepidopterous organisms [68]. Similar molecular modling of AChE-1 was geterated to investigate resistance associated mutation in R. microplus.…”

In silico modeling, docking of ThPON1-like protein, and in vitro validation of pesticide tolerance in Trichoderma harzianum

“…Protein modeling, molecular docking, and other high throughput techniques can be employed to predict the biodegradation potential of an organism. In silico bioremediation can address the research gaps and predict the customized degradative enzymes for instantaneous removal of toxic pesticides [20][21][22][23]. In silico analysis of pesticide degradation potential of some bacterial enzymes has been done, but studies with fungi (especially Trichoderma) are very few.…”