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Expression of Aquaporins AaAQP2 and AaAQP6 in the Osmoregulatory Organs of Mosquito Larvae ( Aedes aegypti )
Author(s) -
Guardian Elia Edith Grieco,
Donini Andrew
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.04715
Subject(s) - aedes aegypti , brackish water , biology , osmoregulation , aquaporin , hindgut , salinity , malpighian tubule system , larva , aedes , zoology , ecology , microbiology and biotechnology , midgut
The juvenile stages of the yellow fever mosquito, Aedes aegypti , are found in semi‐permanent water storage containers, septic tanks, and natural coastal rock pools. Changing climates and anthropogenic pollutants affect the ionic (salt) composition of these mosquito breeding sites which can influence the spread and distribution of vector populations. These habitats impose different challenges to the salt and water balance of the mosquitoes which is accomplished by regulation of salt and water transport across epithelial barriers. Aquaporins (AQPs) are transmembrane proteins first discovered as selective water channels and can be classified by their transport capabilities to other small solutes. Six aquaporin isoforms have been identified in A. aegypti mosquitoes, AaAQP1‐6, and here we investigated the protein localization and abundance levels of AaAQP2 and AaAQP6 in the osmoregulatory organs of the aquatic larvae reared in either ion‐poor water (IPW; reverse‐osmosis water), artificial freshwater (FW), or brackish water (BW; 30% seawater). Using custom antibodies with immunohistochemistry and western blotting it was found that AaAQP2‐like and AaAQP6‐like immunofluorescence was primarily intracellular in the Malpighian tubules (MTs) and gastric caeca (GC). Rearing salinity did not affect protein abundance of AaAQP2 in MTs, GC and hindgut which appeared as a putative dimer of ~ 45 to 50 kDa; however, in the hindgut of BW reared larvae an additional band of ~ 30 kDa was apparent which may represent the monomer. Western blots for AaAQP6 are currently being optimized. Results suggest that AaAQP2 and AaAQP6 are required in these osmoregulatory organs regardless of the salinity of the external environment during development. Furthermore, AaAQP2 may have additional functions in the hindgut of larvae that develop in higher salt environments. Support or Funding Information NSERC ‐ DISCOVERY RGPIN‐2018‐05841