Structure, gene expression, and putative functions of crustacean heat shock proteins in innate immunity

Abstract Heat shock proteins (HSPs) are molecular chaperones with critical roles in the maintenance of cellular proteostasis. HSPs, which regulate protein folding and refolding, assembly, translocation, and degradation, are induced in response to physiological and environmental stressors. In recent years, HSPs have been recognized for their potential role in immunity; in particular, these proteins elicit a variety of immune responses to infection and modulate inflammation. This review focuses on delineating the structural and functional roles of crustacean HSPs in the innate immune response. Members of crustacean HSPs include high molecular weight HSPs (HSP90, HSP70, and HSP60) and small molecular weight HSPs (HSP21 and HSP10). The sequences and structures of these HSPs are highly conserved across various crustacean species, indicating strong evolutionary links among this group of organisms. The expression of HSP-encoding genes across different crustacean species is significantly upregulated upon exposure to a wide range of pathogens, emphasizing the important role of HSPs in the immune response. Functional studies of crustacean HSPs, particularly HSP70s, have demonstrated their involvement in the activation of several immune pathways, including those mediating anti-bacterial resistance and combating viral infections, upon heat exposure. The immunomodulatory role of HSPs indicates their potential use as an immunostimulant to enhance shrimp health for control of disease in aquaculture.