Molecular cloning and functional analysis of nucleotide-binding oligomerization domain 1 (NOD1) in olive flounder, Paralichthys olivaceus.

Abstract

The gene encoding nucleotide-binding oligomerization domain 1 (NOD1) was cloned from olive flounder (Paralichthys olivaceus) and the role played by NOD1 during Edwardsiella tarda infection was evaluated. The complete open reading frame of NOD1 was 2820 bp in length, encoding a 939-amino acid polypeptide. The NOD1 protein contains three conserved domain structures including C-terminal LRRs, a central NACHT motif, and an N-terminal CARD domain, which show similarities of 49-74% to those of other vertebrate counterpart proteins. NOD1 expression was observed in all fish tissues examined, and the levels increased in olive flounder infected with E. tarda, Streptococcus iniae, or viral hemorrhagic septicemia virus (VHSV). When hirame natural embryo (HINAE) cells over-expressing NOD1 were infected with E. tarda, bacterial growth was inhibited, and the IL-1β transcript level increased compared to that of the control. These findings imply that NOD1 plays an important role in response to E. tarda infection of olive flounder.