HSP40 mediated TLR-Dorsal-AMPs pathway in Portunus trituberculatus

Heat shock protein 40 (HSP40) is a kind of molecular chaperone involved in various immune responses. How-ever, the exact roles of HSP40 in immune defense against bacteria remain largely unclear. In this study, the activation function of a type I HSP40 from Portunus trituberculatus (PtHSP40-I) in the TLR pathway was inves-tigated. The results showed that PtHSP40-I can bind to lipopolysaccharide (LPS) and peptidoglycan (PGN). The PtHSP40-I also exhibited binding activity toward the extracellular leucine-rich repeat (LRR) domain of Toll-like receptor (TLR). Moreover, the PtHSP40-I could promote the transcription factor Dorsal translocated from cytoplasm into the nucleus in hemocytes and participated in regulating the expression of anti-lipopolysaccharide factor (ALF) and crustin. These findings provided insights into the activation mechanisms of TLR pathway mediated by HSP40 and offered basic theory of disease control in P. trituberculatus aquaculture.

Automated summary

This study investigated the activation function of a type I heat shock protein 40 (PtHSP40-I) from Portunus trituberculatus in the TLR pathway. The results showed that PtHSP40-I can bind to lipopolysaccharide and peptidoglycan, and also exhibit binding activity towards the extracellular leucine-rich repeat domain of Toll-like receptors. Moreover, PtHSP40-I promotes the translocation of the transcription factor Dorsal and participates in regulating the expression of anti-lipopolysaccharide factor and crustin. These findings provide insights into the activation mechanisms of the TLR pathway mediated by HSP40 and have implications for disease control in P. trituberculatus aquaculture.