Serum amyloid P-component/C-reactive proteins in fugu (Takifugu rubripes) egg with binding ability to disease-causing bacteria by carbohydrate-recognition

Two galactose-binding proteins were purified from the eggs of Takifugu rubripes by affinity chromatography. These proteins were detected at 26 and 23 kDa under reducing and at 40 and 45 kDa under non-reducing conditions at SDS-PAGE. The peptide sequences from both proteins matched to short-type pentraxin. The 26-kDa lectin was glycosylated, while the other one was not, indicating that these could be glycoforms of pentraxin. Messenger RNA of pentraxin was detected in eggs and embryos at 1-cell stage, was undetectable fill blastula, and finally detected again after gastrula, suggesting that the mRNAs in eggs and 1-cell embryos were maternal in origin, and autologous transcription of the gene occurred after blastula. Since they bind to pathogenic bacteria, egg pentraxin may have immunological functions during embryogenesis. This is the first study to show the presence of short-type pentraxin in fish eggs and the diversity of fish egg lectins.