Abstract
The vitellogenin receptor (VgR) functions as an essential component in uptaking and transporting vitellogenin (Vg) in female adults, which is involved in ovary development and oviposition. This study aimed to clarify the molecular characteristics and function of VgR in the oriental fruit fly Bactrocera dorsalis (Hendel). Here, we identified the full-length of BdVgR (GenBank Accession No. JX469118), encoding a 1925 residue (aa) protein with a 214.72 kDa molecular mass and several typical motifs of low-density lipoprotein receptor superfamily (LDLR). Phylogenic analysis suggested that BdVgR was evolutionary conserved with other Dipteran VgRs. The expression of BdVgR was exclusively detected in the ovaries rather than head, thorax or other tissues. The developmental expression patterns showed that the signal of BdVgR was detectable in very beginning of adult stage, and positively correlated with the growth rate of ovaries and the expression levels of its ligands. In addition, we also demonstrated that the expression level of BdVgR, and ovary development were significantly suppressed after being injected with BdVgR-targeted dsRNA. Together, all of these results indicated that BdVgR was critical for yolk protein absorption and ovary maturation in B. dorsalis, playing a vital role in female reproduction.
Highlights
In insects, including oviparous species, successful reproduction is fundamental in maintaining their population, which relies on two key indispensable steps: vitellogenin (Vg) biosynthesis and deposition.After being synthesized in the fat body and released into the hemolymph, Vg is taken up into the developing ovaries via endocytosis by its receptor, vitellogenin receptor (VgR), which is located on the surface of the oocytes within clathrin-coated pits [1]
This lipoprotein is transported to its target recipient cell by VgR, providing multiple nutritional elements to support the developments of oocytes [2]
In silico analysis further suggests that insect VgR is a member of the low density lipoprotein receptor (LDLR) superfamily, which is characterized by five highly conserved, but functionally different, amino acids domains: the ligand-binding domain (LBD) containing several Class A cysteine-rich repeats (LDLRA), the epidermal growth factor (EGF)-precursor domain comprising Class B cysteine-rich (LDLRB, EGF-like repeats) and YWXD repeats, the O-linked sugar domain, the transmembrane domain, and the cytoplasmic tail domain with internalization signals [3]
Summary
After being synthesized in the fat body and released into the hemolymph, Vg is taken up into the developing ovaries via endocytosis by its receptor, vitellogenin receptor (VgR), which is located on the surface of the oocytes within clathrin-coated pits [1]. This lipoprotein is transported to its target recipient cell by VgR, providing multiple nutritional elements to support the developments of oocytes [2]. There is not enough available information to get the full understanding of the reproductive mechanism of this order, considering its economic importance
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