Abstract
Ferritin is required for iron storage in vertebrates and for iron transport and storage in invertebrates, specifically insects. Classical ferritins consist of 24 subunits configured as a polyhedron wherein iron is held. The 24 subunits include light and heavy chains, each with specific functions. Several homologues of the light and heavy chains have been sequenced and studied in insects. In addition to iron transport and storage, ferritin has a role in dietary iron absorption, and functions as a protective agent preventing iron overload, decreasing oxidative stress, and reducing infection in these animals. The expression profile and regulation of a second ferritin light chain homologue (LCH2) in Aedes aegypti [Linnaeus (Diptera: Culicidae), yellow fever mosquito] was characterized in cells, animal developmental stages, and tissues post bloodmeal (PBM) by real-time PCR and immunoblot. Two previously studied ferritin subunits from Ae. aegypti, HCH and LCH1, along with LCH2 were immunoprecipitated and analyzed by mass spectrometry. The three Ae. aegypti ferritin subunits, HCH, LCH1, and LCH2, have different expression profiles and regulation with iron exposure, developmental stage, and tissue response PBM. Ae. aegypti expresses multiple and unique ferritin light chain subunits. Ae. aegypti, the vector for Zika, Dengue, and yellow fever, requires iron for oogenesis that is transported and stored in ferritin; this vector expresses a second light chain ferritin subunit homologue unlike any other species in which ferritin has been studied to date.