Teleostean IL11b exhibits complementing function to IL11a and expansive involvement in antibacterial and antiviral responses.

Interleukin 11 is a class-1 helical cytokine, having the four-helix bundle structure, possessing pleiotropic characteristics involved in physiological processes including blood production, bone formation and placentation. The interleukin 11 paralogues (IL11a and IL11b) have been identified in fish with only IL11a from carp and trout have been characterized and analyzed for its expression thus far. Here, we cloned and studied the structure and expression of IL11b in Japanese flounder (Paralichthys olivaceus), and compared this with the existing information on fish IL11 paralogues. Japanese flounder IL11b (poIL11b) cDNA is composed of 1536 bp encoding for 201 aa residues with a 23 aa leader peptide, three cysteine residues (C12, C183 and C198) and four potential N-linked glycosylation sites. poIL11b does not show constitutive expression in tissues of adult fish except for the very slight expression in kidney and spleen, and the very high expression in peripheral blood leukocytes (PBLs). poIL11b is transiently up-regulated by bacterial lipopolysaccharide (LPS) and increasingly stimulated by the IFN inducer poly I:C in kidney, spleen and peripheral blood leukocytes of adult fish in vitro. It is likewise slightly stimulated by Edwardsiella tarda infection but is highly expressed after hirame rhabdovirus (HIRRV) infection in kidney of juvenile fish. The stimulation studies suggest that poIL11b, aside from its role in bacterial infection, is well involved in antiviral responses. Moreover, poIL11b structure and expression pattern appears to be slightly distinct and opposite to IL11a, respectively, suggesting a complementation of function of the duplicate fish IL11 genes.