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The first CUB-domain containing serine protease from Chlamys farreri which might be involved in larval development and immune response
- Yang, Chuanyan, Wang, Leilei, Zhang, Huan, Yi, Qilin, Wang, Lingling, Wang, Hao, Song, Linsheng
- Developmental and comparative immunology 2017 v.76 pp. 163-168
- Azumapecten farreri, adults, amino acids, bacteria, beta-glucans, complementary DNA, eggs, fungi, gene expression, gills, hemocytes, hepatopancreas, immune response, kidneys, larvae, larval development, lipopolysaccharides, messenger RNA, open reading frames, peptidoglycans, phylogeny, polypeptides, scallops, serine proteinases, tissues
- Serine proteases (SPs) are one of the most well understood enzyme families, which play an important role in regulating many physiological events. In the present study, one CUB-domain containing serine protease was identified from Chlamys farreri (designated as CfCUBSP). The full-length cDNA of CfCUBSP was of 3181 bp with an open reading frame of 2688 bp encoding a polypeptide of 896 amino acids. CfCUBSP shared closer phylogenetic relationship with those multi-domain SPs which consisted of one SP domain, and different numbers of CUB domain and LDLa domain than other SPs. The mRNA transcripts of CfCUBSP were detected in all developmental stages with the highest expression level in fertilized eggs and the lowest in trochophore larvae. In adult scallop, the CfCUBSP mRNA could be detected in all examined tissues with the highest level in hepatopancreas, and CfCUBSP protein was dominantly located in the gills, hepatopancreas, gonad and kidney. The mRNA expression of CfCUBSP in hemocytes was significantly up-regulated after the stimulation of lipopolysaccharide (LPS), peptidoglycan (PGN) and β-glucan (GLU) (P < 0.05). All the results collectively indicated that CfCUBSP was a primitive member of the invertebrate SPs which might be involved in larval development and immune response against Gram-negative (G−) and Gram-positive (G+) bacteria and fungus in scallop.