The molecular evolution and function of aquaporins in the parasitic salmon louse in relation to its host the Atlantic salmon
| Autor: | Finn, Roderick N., Stavang, Jon A., Chauvigné, François, Nilsen, Frank, Cerdà, Joan |
|---|---|
| Rok vydání: | 2015 |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname |
| Popis: | Jornada Anual de la Secció d’Aqüicultura de la Societat Catalana de Biologia, Avenços en Recerca en Aqüicultura, 12 de Juny de 2015, Barcelona.-- 1 page The saltwater salmon louse (Lepeophtheirus salmonis) is an ectoparasitic crustacean copepod that causes severe infections of salmonids across the Atlantic and Pacific regions. Increasing levels of resistance to established drugs requires alternative approaches to solving the salmon louse epidemic. In contrast to its salmonid host, which is an osmoregulator, the louse´s cell volume regulation breaks down in fresh and brackish waters. These features suggest that aquaporins, which facilitate the transmembrane transport of water and other small uncharged solutes could represent potential therapeutic targets. However almost nothing is known concerning the functional diversity of aquaporins in crustaceans. To redress this lack of knowledge, we screened the genomes of the salmon louse and the Atlantic salmon and phylogenetically characterised their aquaporin superfamily repertoires in relation to those present in 131 arthropod and 121 vertebrate genomes. Subsequently we isolated and cloned seven full-length aquaporin transcripts from the louse and determined the functional transport properties of the encoded channels using a heterologous Xenopus laevis oocyte expression system. Our data reveal that the aquaporin repertoires in crustaceans and other arthropods can be classified into 3 major grades of aquaporins (1) classical type aquaporins including Big brain and Prip-like channels (2) aquaglyceroporins and (3) unorthodox aquaporins, while vertebrates have an additional Aqp8-type grade of channels. Functional characterization of the louse channels, reveal that the permeation properties of the arthropod grades of aquaporin are largely conserved to the vertebrate counterparts. Transcript abundance analyses and subcellular localisation studies indicate that selective aquaporins may be suitable as therapeutic targets |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|