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Lipophorin is the major hemolymph protein responsible for lipid transport among tissues of insects. This protein may be a lipid source for the development and reproduction of human malaria parasites in mosquitoes, and therefore could be a target to disrupt malaria parasite development in the vector. The lipophorin of Anopheles gambiae was purified by KBr gradient ultracentrifugation and showed variation in density from 1.111 to 1.143 g/ml during development. The amount and density of lipophorin increase in blood-fed females, indicating an adaptation of vitellogenic mosquitoes to an elevated rate of lipid transport to the developing eggs. The A. gambiae lipophorin gene is composed of eight exons and transcribes an mRNA that is 10,516 nucleotides in length. The predicted initial translation product is a preproapoliphorin consisting of 3332 amino acids, which is processed by proteolysis to generate two mature apolipophorins: apolipophorin-I (Mr = 280,000) and apolipophorin-II (Mr = 81,000). The gene is expressed in the fat body tissues throughout development. An elevated transcriptional activity of the lipophorin gene during vitellogenesis is consistent with the presence of putative cis-regulatory elements (GATA and ecdysone responsive elements) in its 3'-end flanking DNA sequence.

Original publication




Journal article


Comp Biochem Physiol B Biochem Mol Biol

Publication Date





101 - 109


Amino Acid Sequence, Animals, Anopheles, Apolipoproteins, Base Sequence, Blotting, Northern, Enzyme-Linked Immunosorbent Assay, Female, Gene Expression Regulation, Insect Vectors, Lipid Metabolism, Lipoproteins, Mice, Molecular Sequence Data, Protein Precursors, Rabbits, Reverse Transcriptase Polymerase Chain Reaction, Ultracentrifugation, Vitellogenesis