Research Projects

Aedis and Anopheles spp., the primary vectors for arboviral-borne diseases exhibit high adaptability and thus resilience to mosquito-eradication programs. Aedis spp are more resistant to desiccation stress accounting for its widespread transmission and ineffective vector-control strategies. Aquaporins (AQP) or water channel proteins maintain H2O homeostasis, glycerol and urea transport and dessication tolerance in the haematophagous insect. Insect diapausal stages exhibit decreased H2O loss rates by regulation of AQP expression. The dessication-tolerance of diapausal Aedis eggs thus could be governed by their AQPs. Given this crucial role played by these proteins in the life cycle of a mosquito, it is imperative to develop a thorough understanding of the structure and function of the same, to delineate its potential to be a target for vector control agents. Understanding the fundamental mechanism of AQP function in mosquito eggs requires a detailed biophysical characterization which necessitates cloning of specific AQPs. An in-silico study done by us reveal the presence of AQPs in mosquitoes with less than 30% sequence similarity to their human and Drosophila counterparts. AQP6 is one such AQP we have cloned from Aedis spp which has a high level of selectivity in the Aedes family. However, very less information is available either on the structure or the function of AQP6 in the various developmental stages of the Aedis mosquito. In this project we propose to conduct a structure-function study on Aquaporin AQP6 by functional bioassays and studying its role in dessication-tolerance by knockdown experiments. The results of this study would help infer the potential selection of this group of proteins as a target in vector control programs. In addition, the importance of water-homeostasis and the underlying molecular players in this mechanism would be characterised in Aedis spp. Such an understanding is important in identifying potential interventions to prevent vector borne diseases plaguing mankind.