• DOI:10.1073/PNAS.93.17.8934
• Corpus ID: 35320762

Molecular characterization of the mosquito vitellogenin receptor reveals unexpected high homology to the Drosophila yolk protein receptor.

@article{Sappington1996MolecularCO,
  title={Molecular characterization of the mosquito vitellogenin receptor reveals unexpected high homology to the Drosophila yolk protein receptor.},
  author={Thomasw . Sappington and Vladimir A. Kokoza and W L Cho and Alexander S. Raikhel},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1996},
  volume={93 17},
  pages={
          8934-9
        }
}

• T. W. Sappington, V. Kokoza, +1 author A. Raikhel
• Published 20 August 1996
• Biology
• Proceedings of the National Academy of Sciences of the United States of America

The mosquito (Aedes aegypti) vitellogenin receptor (AaVgR) is a large membrane-bound protein (214 kDa when linearized) that mediates internalization of vitellogenin, the major yolk-protein precursor, by oocytes during egg development. We have cloned and sequenced two cDNA fragments encompassing the entire coding region of AaVgR mRNA, to our knowledge the first insect VgR sequence to be reported. The 7.3-kb AaVgR mRNA is present only in female germ-line cells and is abundant in previtellogenic oocytes, suggesting that the AaVgR gene is expressed early in oocyte differentiation. The deduced amino acid sequence predicts a 202.7-kDa protein before posttranslational processing. The AaVgR is a member of the low density lipoprotein receptor superfamily, sharing significant homology with the chicken (Gallus gallus) VgR and particularly the Drosophila melanogaster yolk protein receptor, in spite of a very different ligand for the latter. Distance-based phylogenetic analyses suggest that the insect VgR/yolk protein receptor lineage and the vertebrate VgR/low density lipoprotein receptor lineage diverged before the bifurcation of nematode and deuterostome lines.