Abstract

High-mobility group box 1 (HMGB1) is a highly conserved nuclear protein and participates in the immune response to pathogens in bony fish. In this study, the structure and function of HMGB1 in the cyprinid fish Schizothorax prenanti (SpHMGB1) were investigated. The spatial structure of SpHMGB1 was predictedbyCPHmodels. Quantitative reverse transcription PCR was used to detect the mRNA of SpHMGB1 in different tissues and Streptococcus agalactiae infection. The macrophage was treated with synthetic SpHMGB1-B box peptide to analyze the inflammatory activity. Structurally, SpHMGB1 had the conserved A box, B box, and acid tail compared with Zebrafish Danio rerio and mice Mus musculus. SpHMGB1 was universally expressed in various tissues, with the highest expression in the middle kidney. In vivo, SpHMGB1 was significantly induced in response to Streptococcus agalactiae infection in the blood and spleen. Synthetic SpHMGB1-B box peptide activated respiratory burst and up-regulated the messenger RNA expression of interleukin-1β, tumor necrosis factor α, interleukin-10, interferon regulatory factor 1, interferon regulatory factor 7, C-X-C motif chemokine ligand 11-1, C-X-C motif chemokine ligand 11-2, and toll-like receptor 4 in macrophages. This study suggested that SpHMGB1 participated in the response to bacterial pathogens and that SpHMGB1-B box peptide played an important role in mediating the immune response of S.prenanti.

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