Submitted to: Immunology Research Workshop
Publication Type: Abstract Only
Publication Acceptance Date: 12/1/2003
Publication Date: 12/1/2003
Citation: Wiens, G.D., Palti, Y., Rexroad III, C.E., Welch, T.J. 2003. Molecular characterization of a putative tumor necrosis factor superfamily 13b (tnfsf 13b) homologue from rainbow trout (oncorhynchus mykiss). Immunology Research Workshop. p.35.
Technical Abstract: Little is known about the immune system function of economically important cool and cold water fish species. Such knowledge is important for developing successful vaccines and disease resistant fish. In mammals, members of the tumor necrosis factor superfamily (TNFSF) play important roles in both innate and adaptive immune responses. In order to determine which TNFSF members are conserved and expressed in rainbow trout, we have searched a computer database of ~50,000 expressed sequence tags generated at the National Center for Cool and Cold Water Aquaculture. We have identified 17 cDNAs that have homology to known TNFSF ligands or receptors. Here, we describe one cDNA, 1RT126I22, which has homology to TNFSF 13b. TNFSF 13b is also known as B-cell activating factor (BAFF) or B-lymphocyte stimulating factor (BLYS). In mice and humans, TNFSF 13b is produced by myeloid cells and is critical for mature B cell survival and antibody production. The rainbow trout cDNA, 1RT126I22, encodes a predicted 141 amino acid protein, which shares 54% amino acid identity with human TNFSF13b, 51% identity with mouse TNFSF13b, and 54% identity with chicken TNFSF13b. The rainbow trout TNFSF 13b shares 100% identity with a 99 amino acid protein predicted from a truncated Atlantic salmon cDNA, and 78% identify with puffer fish TNFSF13b protein predicted from genomic DNA sequence. The rainbow trout TNFSF 13b is unusual as it does not possess a transmembrane domain or a furin-type protease cleavage site characteristic of the human, mouse, and chicken TNFSF 13b molecules. Examination of rainbow trout TNFSF 13b gene expression during vaccination and bacterial challenge is underway. To our knowledge, this is the first identification and characterization of fish TNFSF 13b homologues.