Article ID Journal Published Year Pages File Type
2433632 Fish & Shellfish Immunology 2007 9 Pages PDF
Abstract

The α-chain of IL-15 receptor complex serves as a high-affinity, specific subunit for IL-15 binding. It shares functional and structural features with IL-2 receptor α-chain. Here we report for the first time that the molecular cloning, characterization and sequence analysis of the teleostean IL-15Rα from Oncorhynchus mykiss. The full-length cDNA comprises of a 5′ untranslated region (UTR) of 167 bp, an open reading frame of 732 bp and a large 3′UTR of 630 bp, constitutively expressed in all the tissues examined. Another two variants are found derived from alternative splicing. Two copies of rainbow trout IL-15Rα (rtIL-15Rα) were detected in the genome by Southern blot hybridization. Moreover, EST evidence is also traced from other fishes. The deduced rtIL-15Rα of 243 amino acids contains a 17aa signal peptide at N-terminus and a transmembrane region at C-terminus, as well as a typical sushi domain included in the extracellular region. Phylogenetic tree analysis groups rtIL-15Rα with other IL-15Rαs but separates it from IL-2Rαs. In addition, a putative sequence was found in the sushi domain which is conserved and versatile among all species and this might relate to cytokine recognition.

Related Topics
Life Sciences Agricultural and Biological Sciences Aquatic Science
Authors
, , ,