Abstract

Vitellogenin receptor plays a key role in the embryonic development of oviparous animals. A vitellogenin receptor (VgR) gene was cloned from Actias selene using reverse transcriptase-polymerase chain reaction and rapid amplification of cDNA end PCR. Sequence analysis revealed that this gene was 5848 bp and encoded a protein of 1812 amino acids peptide with high similarity to Bombyx mori VgR. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blotting analysis demonstrated that a 24 and 40 KD recombinant proteins corresponding to the ligand-binding domains of A. selene VgR was successfully expressed in Escherichia coli cells. 

Key words: Actias selene Hubner, vitellogenin receptor (VgR), prokaryotic expression.