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Sci Rep
2015 Jan 15;5:7795. doi: 10.1038/srep07795.
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Functional characterization of aquaporins and aquaglyceroporins of the yellow fever mosquito, Aedes aegypti.
Drake LL
,
Rodriguez SD
,
Hansen IA
.
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After taking vertebrate blood, female mosquitoes quickly shed excess water and ions while retaining and concentrating the mostly proteinaceous nutrients. Aquaporins (AQPs) are an evolutionary conserved family of membrane transporter proteins that regulate the flow of water and in some cases glycerol and other small molecules across cellular membranes. In a previous study, we found six putative AQP genes in the genome of the yellow fever mosquito, Ae. aegypti, and demonstrated the involvement of three of them in the blood meal-induced diuresis. Here we characterized AQP expression in different tissues before and after a blood meal, explored the substrate specificity of AQPs expressed in the Malpighian tubules and performed RNAi-mediated knockdown and tested for changes in mosquito desiccation resistance. We found that AQPs are generally down-regulated 24 hrs after a blood meal. Ae. aegypti AQP 1 strictly transports water, AQP 2 and 5 demonstrate limited solute transport, but primarily function as water transporters. AQP 4 is an aquaglyceroporin with multiple substrates. Knockdown of AQPs expressed in the MTs increased survival of Ae. aegypti under dry conditions. We conclude that Malpighian tubules of adult female yellow fever mosquitoes utilize three distinct AQPs and one aquaglyceroporin in their osmoregulatory functions.
Figure 1. Aedes aegypti AQP expression in various parts of the alimentary canal.Expression was assayed using qPCR. The data represent relative quantification of Aedes AQPs which were normalized by qPCR analysis of ribosomal protein S7 (rpS7) mRNA levels in the cDNA samples. Values are means ± S.E. (error bars) of triplicate biological samples. The Y-axis shows expression ratios in arbitrary units with the lowest expressing tissue set as 1. Means separated by Tukey–Kramer HSD (p < 0.05). Means which share the same letter are not significantly different. RNA was isolated from organs/body parts of adult female mosquitoes unfed (light shaded columns) and 24 hrs after a blood meal (dark shaded columns). C-crop, FG-foregut, MG-midgut, HG-hindgut, R-rectum, MT – Malpighian tubules, OV – ovaries.
Figure 2. Water permeability analysis of Ae.
aegypti AQPs expressed in Xenopus
laevis oocytes.(a) Day 3 post-injection with AQP cRNA, Western blot analyses of oocyte lysates using Myc-tag antibody (the AQP tetramer band is shown). The blots were cropped, and the full-length blots are presented in the supplementary information (see Supplementary Fig. S1). (b) Effect of heterologous expression of Aedes AQPs on water permeability of Xenopus oocytes. The light-shaded columns represent oocytes that were pre- treated with HgCl2. Each AQP group n = 9, and their mean separated by Tukey–Kramer HSD (p < 0.05). Means which share the same letter are not significantly different.
Figure 3. Various solute transport capabilities of Ae.
aegypti AQPs expressed in Xenopus laevis oocytes.Solute uptake was reported as an oocyte swelling rate [d(V/V0)/dt] and measured in μm/sec. There were six solutes tested, in each AQP group n = 5. The molecular structure of each solute is indicated above each graph. The means were separated by the Tukey-Kramer HSD (p < 0.05). Means which share the same letter are not significantly different.
Figure 4. RNAi-mediated knockdown of Ae.
aegypti AQPs demonstrate desiccation resistance.Effect of RNAi-mediated AQP knockdown on Aedes survival under desiccation conditions. AQP 1, 4 and 5 knockdown mosquitoes have a significant increase in survival compared to the eGFP control group. Kaplan-Meier and log-rank tests were performed using Graphpad Prism software.
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