Genomic structure, molecular characterization and functional analysis of Pekin duck interleukin-10

Here we describe the cloning and expression of Pekin duck IL-10 (duIL-10) and a six exon-5 intron structure of an IL-10 gene. Two transcripts encoding duIL-10 with an alternatively spliced 3′UTR, and a transcript lacking exon 5 with a novel coding sequence for its C-terminus (duIL-10ΔE5) were isolated from splenocytes. The duIL-10 protein has an amino acid identity of 79% and 47% with chicken and human IL-10, respectively. The duck IL-10 gene shares a similar structure of the respective exons 1–5 with the IL-10 genes of other vertebrates but has an alternative exon. The duIL-10 3D structure by homology modeling was similar to that of the human IL-10 monomer, whereas the predicted duIL-10ΔE5 protein lacks helix F. DuIL-10 and duIL-10ΔE5 transcripts were most abundant in primary and secondary immune organs and lung. Recombinant duIL-10 suppressed duck IL-2 transcripts in mitogen-activated PBMCs. Our observation suggests evolutionary conservation of structure and function of the duIL-10 protein but the roles of the novel IL-10 splice variants in the regulation of duck immune responses and evolution of vertebrate immunity remain to be elucidated.

► This study is the first characterization of interleukin (IL)-10 in the Pekin duck.
► The duck IL-10 gene has an alternative exon.
► It gives rise to two novel alternatively spliced IL-10 transcripts.
► IL-10 transcripts were most abundant in lung, bursa, cecal tonsils, spleen and liver.
► Bioactivity of recombinant duck IL-10 was shown by an IL-2 mRNA repression assay.