T-108-16
Characterization and Functional Expression Analysis of IL-10 in Seriola dumerili
M. Tanekhy, A. Yamamoto, K. Araki
In mammals, interleukin-10 is a potent regulatory cytokine with pleiotropic effects on various leukocytes. In the present study, seiola dumerili IL-10 (sdIL-10) has been identified and recombinant sdIL-10 (rsdIL-10) was prepared by using a prokaryotic expression system. The sdIL-10 gene encodes a 187 amino acid protein and comprises a five exon-four intron structure as other known IL-10 genes. Important structural residues are maintained in the sdIL-10 protein, including the four cysteines responsible for the two intra-chain disulfide bridges reported for human IL-10. The 3D structure of sdIL-10 was predicted. This first homology model of a fish IL-10 reveals a high degree of compatibility between the dimeric quaternary architectures of sdIL-10 and its mammalian counterparts. The phylogenetic analysis clusters sdIL-10 with other IL-10s, apart from IL-10-related molecules. The involvement of IL-10 in Seriola dumerili immune responses was demonstrated by investigating the expression profiles of IL-1β and IL-10 in the head-kidney and spleen following intraperitoneal injection of FCK live Nocardia Seriola. These results provide clues to the potential immunoregulatory role and production of IL-10 in teleost.