Abstract
CD38 is a multifunctional cell surface molecule that plays a crucial role in B cell activation, differentiation, and maturation in mammals with an increased expression in B cell maturation. In this study, a CD38-like molecule (OnCD38) was cloned and identified from Nile tilapia (Oreochromis niloticus), and its functional characterization was investigated. The open reading frame of OnCD38 is 828 bp of the nucleotide sequence, encoding a polypeptide of 275 amino acids. The deduced amino acid sequence of OnCD38 is highly homologous to other teleost fish and similar to mammals, containing extracellular, intracellular and transmembrane regions. Subcellular localization studies revealed that OnCD38 molecules were presented on the surface of B cells. Three healthy tilapia were used in each experimental group and control group. Following keyhole limpet hemocyanin (KLH) challenge in vivo, the mRNA expression of OnCD38 was significantly up-regulated in peripheral blood, spleen, and head kidney, with an earlier up-regulation in the second challenge than the first one. The up-regulation of OnCD38 expression was also detected in head kidney leukocytes after stimulation with LPS, recombinant HomoIL-10 ((r)HomoIL-10), (r)OnIL-10, and LPS plus (r)OnIL-10 in vitro. Furthermore, the OnCD38 expression increased with the differentiation of B cells, reaching a high level (10.1 fold higher than resting mature B cells) at the plasma-like B cells. Taken together, in this study, these results indicate that the OnCD38 is likely involved in the T cell-dependent response and plays roles in B cell differentiation in Nile tilapia.
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