bioRxiv Science⌕ Search

bioRxiv · 10.1101/2020.08.07.241224

Determination of the amount of insecticide picked up by mosquitoes from treated nets

Abstract

BackgroundInsecticides used in vector control mostly rely on vectors being exposed through contact with treated surfaces, yet little is known about the amount picked up by the insect. Measuring this amount is relevant not only for determining the actual doses that are lethal to the mosquito, but also for understanding effects on the physiology and vector competence of mosquitoes. Insecticides at sub-lethal doses can affect both parasites developing inside mosquitoes and mosquito microbiota, hence it is important to understand the processes by which parasites are exposed to insecticide inside the insect. These doses will inevitably depend on the amount of insecticide that mosquitoes pick up when they come into contact with treated nets. MethodsThree to five days old non-blood fed female Anopheles coluzzii mosquitoes were exposed to a long-lasting insecticidal net (PermaNet 2.0 containing 55 mg/m2 deltamethrin), using a wire ball frame, for 0.5-5.0 minutes. Our in-house developed colorimetric test was used to visually detect the amount of deltamethrin on different parts of the mosquito (legs, heads, thoraxes, abdomens) following exposure to the net. The amount of insecticide picked up by mosquitoes from the net over a range of exposure times was measured using a high-performance liquid chromatography with diode array detection (HPLC-DAD). ResultsThe colorimetric test, designed to only detect the type 2 pyrethroids (i.e deltamethrin, -cypermethrin and {lambda}-cyhalothrin) on fabrics (e.g. ITNs) and sprayed walls, was successfully used for the first time to detect deltamethrin on mosquitoes following exposure to the net. The confirmatory HPLC-DAD analysis determined that after 2 min exposure up to 12 ng of deltamethrin adhered to mosquitoes following exposure to PermaNet 2.0 (mean = 5.2 ng/mosquito, SE = 1.9) and that the final dose depends on the length of exposure time. ConclusionsThis study demonstrated the potential of a screening (type 2 pyrethroid colorimetric test) and a confirmatory test (HPLC-DAD) to determine the amount of insecticide that adheres to mosquitoes on contact with treated surfaces. This has implications for a precise lethal dose determination and detection of specific insecticide that causes the greatest mosquito mortality in circumstances where mixtures of insecticides may be used to maximise effectiveness of interventions.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Kristan, M., Lines, J., Kaur, H.. 2020-08-07. Determination of the amount of insecticide picked up by mosquitoes from treated nets. https://doi.org/10.1101/2020.08.07.241224

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

EngA adopts multiple distinct conformational states during ribosome assembly

Ribosome assembly, a highly coordinated and crucial cellular process, is assisted by various assembly factors, including GTPases. EngA, an essential P-loop GTPase, is involved in late-stage assembly of the 50S ribosomal subunit. The structures of 50S ribosome in complex with EngA-bound GMPPNP, and EngA-bound GDP alone, without 50S subunit, have been reported previously. However, the molecular mechanism of EngA GTP hydrolysis-assisted 50S maturation remains poorly understood, and structures of the 50S ribosome in complex with EngA-bound GDP have yet to be deciphered. We have reported cryo- EM structures of the Mycobacterium smegmatis 50S ribosome in complex with EngA-bound GTP{gamma}S or GDP at 2.8 - 3.5 [A] resolution. Structural analysis revealed that EngA and 50S subunit undergo a coordinated structural rearrangement, and an assembly intermediate is formed in which the stem-loop of H80 makes base-pair interactions with the junction of H89 and H90, forming a unique stem-loop-junction (SLJ) motif. EngA-bound GDP adopts distinctly different conformations in its ribosome-bound and unbound states. In summary, this study proposed a multi-state conformational model for EngA-assisted ribosome assembly.

biochemistry↗

Modular assembly of mitochondrial complex III from a dynamic matrix domain pool

Mitochondrial complex III is a central component of the cellular energy metabolism. It is an obligate dimer of catalytic and accessory subunits that are encoded by two genomes. How its large matrix domain, formed by the core proteins Qcr1 and Qcr2, is built and joined to the membrane part and during assembly is not known. Here we show that Qcr1 and Qcr2 preassemble independently of complex III into matrix domain modules. Cryo-EM structures from a cardiolipin-deficient yeast strain and of recombinant protein resolved single, double and triple matrix domains, which are linked by the C-terminal tail of Qcr1. In the mature complex III, the same tail binds cytochrome b and cardiolipin. The modules form a dynamic pool, in which assembly species interconvert and exchange subunits. Mutations at the module interfaces, including mimics of human disease variants, reshape this pool and deletion of the Qcr1 tail impairs respiratory growth. Substitution of a tyrosine residue linked to parkinsonism exposes a conserved cysteine residue to oxidation. A cryo-EM structure of an assembly intermediate shows a cap of two matrix domains bound to a monomeric membrane module of cytochrome b, Qcr7, Qcr8 and cytochrome c1. We propose that complex III receives its matrix domain from a dynamic pool of prebuilt modules, which organizes the dimerization of the complex.

biochemistry↗

Vasopressin V2 receptor phosphopeptide reshapes the conformational landscape of arrestin-2 beyond C-tail detachment

Binding of phosphorylated GPCR tails influences arrestin conformation, but the contribution of this interaction to the interdomain rotation associated with activation remains incompletely characterised. In particular, it remains unclear whether displacement of the arrestin C-tail is sufficient to favor larger interdomain rotations or whether the bound phosphotail exerts an additional effect on the conformational landscape. Here, we used enhanced-sampling simulations to characterise the conformational free-energy landscapes of basal (unbound) and V2Rpp-bound arrestin-2. We find that V2Rpp binding broadened the range of energetically accessible interdomain rotation angles relative to basal arrestin-2. However, the pronounced rotation observed in the experimental structures, while accessible, was not strongly favored. Strikingly, C-tail displacement alone does not reproduce this effect, as arrestin-2 retains a strong preference for small interdomain rotation angles in the absence of V2Rpp. Moreover, the C-tail-detached state is energetically unfavorable in the absence of V2Rpp. Together, these findings quantify the effects of V2Rpp binding on the interdomain rotation of arrestin-2 and disentangle the effects of phosphopeptide binding from those of C-tail detachment.

biochemistry↗