Antibacterial functions of a novel fish-egg lectin from spotted knifejaw (Oplegnathus punctatus) during host defense immune responses.

Fish-egg lectins (FELs) have been identified in several teleost species and have been proved to play important roles in innate immune system against pathogen infection. In this study a novel fish-egg lectin (OppFEL) was identified from spotted knifejaw (Oplegnathus punctatus), and the expression patterns against bacterial infection was characterized. The amino acid sequence is highly homologous to other teleost FELs, containing five repeats of the conserved TECPR domain. Expression of OppFEL was widely observed in examined tissues, with the most abundant transcripts observed in gill, showing a pattern of tissue specific expression. The OppFEL expression was significantly up-regulated following a Gram-negative bacterium (Vibrio anguillarum) challenge in vivo, suggesting participation in host antibacterial immune responses. Recombinant OppFEL protein (rOppFEL) possessed calcium dependent binding capacities and agglutination to four Gram-negative bacterium and two Gram-positive bacterium. Sugar binding assay revealed that rOppFEL specifically bound to insoluble lipopolysaccharide and peptidoglycan. In addition, rOppFEL was also proved to have hemagglutinating activity against erythrocytes from Mus musculus, O. punctatus, Sebastes schlegelii and Paralichthys olivaceus. Dual-luciferase analysis showed that overexpression of OppFEL could suppress the activity of NF-κB in a dose dependent manner. Taken together, these results suggest that OppFEL is a unique fish-egg lectin that possesses apparent immunomodulating property and is involved in host defense against pathogens invasion.