RESUMO
Lipophorin is a major hemolymph lipoprotein found in insects with a molecular native mass of 700 kDa. In mosquitoes, two different types of apolipoproteins are characterized, apolipophorin-I (ApoLp-I, ~250 kDa) and apolipophorin-II (ApoLp-II, ~80 kDa). This concentration depends on the stage of development and the age of the insects. Lipophorins are best studied in mosquitoes of the genus Aedes and Anopheles. In this study, we analyze the lipophorin sequence and show the lipophorin purification of the Culex quinquefasciatus and the transcriptional profile of the lipophorin gene in different life cycle stages. Similar amino acid composition and molecular weights are founded in three mosquitoes species lipophorins amino acid sequence. The two subunits of purified lipophorin (Apo I and Apo II) showed molecular masses of approximately 248 and 93 kDa, like that found in other mosquitoes. A gradual increase in the lipophorin expression gene was obtained during the previtellogenic period and after feeding we obtained peak expression at 24 h after feeding. With our results, we conclude that C. quinquefasciatus protein sequence has the same characteristics as those observed in other mosquitoes and that the expression of its apolipophorins is induced by blood feeding.
