Molecular Cloning of Heat Shock Protein 60 (SpHSP60) from Schizothorax prenanti and the Gene Expressions of Four SpHSPs during Lipopolysaccharide (LPS) Infection

Heat shock proteins (HSPs) play a key role in anti-stress and immune processes are associated with autoimmune diseases. In order to explore the immunological of HSPs from Schizothorax prenanti (S. prenanti), SpHSP60 was cloned for first time this study, gene expressions SpHSP27, SpHSP60, SpHSP70 SpHSP90 hepatopancreas, head kidney, hindgut spleen were analyzed by quantitative real-time PCR (qPCR) after treatment lipopolysaccharide (LPS). The open reading frame (GenBank accession number ON245159) is 1728 bp. It encodes protein 575 amino acids. Its C-terminus highly conserved repeated glycine sequence, which an important cofactor ATP binding. Compared control group, most SpHSPs significantly upregulated tissues examined at 12 or 24 h LPS challenge. abundant expression found kidney injection, followed SpHSP27 h; both these displayed strong under stresses, about 20–70 fold more than that SpHSP90. temporal patterns four SpHSP genes different examined. Taken together, results suggest participate innate immunity stimulated LPS, response intensity organ-specific, indicating they could provide early warning information against bacterial infection. findings our study will contribute better understanding biological roles involved defending pathogenic