Bacteria binding and antibacterial activities of three small heat shock protein from the swimming crab, Portunus trituberculatus

Abstract

The swimming crab, Portunus trituberculatus, is one of the most important commercial crabs cultured in China, with a total yield of approximately 100,000 tons (Fisheries Bureau of Agriculture Ministry of China, 2019). In recent decade, despite the increasing development of the P. trituberculatus farming industry, diseases caused by bacterial infection have caused tremendous economic losses and posed serious threats to the sustainable and healthy development of P. trituberculatus aquaculture industry. Excavating immune-related molecules from host, especially antibacterial molecules, will provide theoretical guidance and candidate therapeutic agents to address the disease problem.Heat shock proteins (HSPs), which widely exist in prokaryotes and eukaryotes, are molecular chaperones that play critical roles in maintaining cellular homeostasis (Schlesinger, 1990;Sikora & Grzesiuk, 2007). According to their homology and molecular mass, HSPs can be grouped into several families, including HSP110, HSP100, HSP90, HSP70, HSP60 and small molecular mass HSPs (sHSPs) (Craig et al., 1994;Tang et al., 2011). HSPs play a primary role