RRC ID 21794
Author Lin Y, Meng Y, Wang YX, Luo J, Katsuma S, Yang CW, Banno Y, Kusakabe T, Shimada T, Xia QY.
Title Vitellogenin receptor mutation leads to the oogenesis mutant phenotype "scanty vitellin" of the silkworm, Bombyx mori.
Journal J Biol Chem
Abstract BACKGROUND:The vitellogenin receptor (VgR) mediates the uptake of vitellogenin (Vg) from the hemolymph by developing oocytes.
RESULTS:VgR with the mutational EGF1 domain can bind ligand proteins but cannot be dissociated under acidic conditions. The mutant is lethal in embryos.
CONCLUSION:Bombyx mori VgR (BmVgR) has an important role in egg formation and embryonic development.
SIGNIFICANCE:BmVgR is a potential target for pest control. In insects, the vitellogenin receptor (VgR) mediates the uptake of vitellogenin (Vg) from the hemolymph by developing oocytes. The oogenesis mutant scanty vitellin (vit) of Bombyx mori (Bm) lacks vitellin and 30-kDa proteins, but B. mori egg-specific protein and BmVg are normal. The vit eggs are white and smaller compared with the pale yellow eggs of the wild type and are embryonic lethal. This study found that a mutation in the B. mori VgR gene (BmVgR) is responsible for the vit phenotype. We cloned the cDNA sequences encoding WT and vit BmVgR. The functional domains of BmVgR are similar to those of other low-density lipoprotein receptors. When compared with the wild type, a 235-bp genomic sequence in vit BmVgR is substituted for a 7-bp sequence. This mutation has resulted in a 50-amino acid deletion in the third Class B region of the first epidermal growth factor (EGF1) domain. BmVgR is expressed specifically in oocytes, and the transcriptional level is changed dramatically and consistently with maturation of oocytes during the previtellogenic periods. Linkage analysis confirmed that BmVgR is mutated in the vit mutant. The coimmunoprecipitation assay confirmed that mutated BmVgR is able to bind BmVg but that BmVg cannot be dissociated under acidic conditions. The WT phenotype determined by RNA interference was similar to that of the vit phenotype for nutritional deficiency, such as BmVg and 30-kDa proteins. These results showed that BmVgR has an important role in transporting proteins for egg formation and embryonic development in B. mori.
Volume 288(19)
Pages 13345-55
Published 2013-5-10
DOI 10.1074/jbc.M113.462556
PII S0021-9258(19)54565-3
Description vit(白妙卵)の原因遺伝子はビテロジェニンレセプターをコードするBmVgRである。d50系統(vit/vit)では、BmVgRのエクソン11に228bpの欠失が存在する。
PMID 23515308
PMC PMC3650373
MeSH Amino Acid Sequence Animals Bombyx / embryology Bombyx / genetics* Cloning, Molecular Egg Proteins / chemistry Egg Proteins / genetics* Egg Proteins / metabolism Embryonic Development Female Gene Knockdown Techniques Genetic Linkage Insect Proteins / chemistry Insect Proteins / genetics* Insect Proteins / metabolism Male Molecular Sequence Data Oogenesis* Organ Specificity Ovary / embryology Ovum / metabolism Ovum / physiology Phenotype Protein Sorting Signals Protein Structure, Tertiary Protein Transport RNA Interference Receptors, Cell Surface / chemistry Receptors, Cell Surface / genetics* Receptors, Cell Surface / metabolism Sequence Deletion Transcription, Genetic Vitellins / metabolism Vitellogenins / metabolism
IF 4.238
Times Cited 45
Silkworms d50