Abstract
Heat shock proteins (HSPs), also known as stress proteins and exogenous chaperone proteins, are a group of highly conserved proteins with different molecular weights, including sHsps, Hsp70, Hsp90, and Hsp60. HSPs are synthesized under normal physiological conditions and in response to stress. As molecular chaperones, HSPs are involved in the folding and assembly of protein polypeptide chains, renaturation of damaged proteins, immune recognition, cell apoptosis, and other physiological activities. In aquatic animals, including fish, crustaceans, and echinoderms, the functions of a variety of Hsp proteins have been reported. In addition to enhancing the anti-stress ability of aquatic animals, Hsps can also play a broader role in various aspects of the epidemic system function, cell apoptosis, and inflammatory process. Exogenous HSPs can also be used as vaccines to increase resistance to pathogens by stimulating the humoral and cellular aspects of the innate immunity of the host. HSPs can also be used as vaccine adjuvant, playing an important role in the development of effective vaccines against aquatic diseases. Therefore, HSPs can be used as an important target site for aquatic animals. By regulating the expression and function of HSPs, it can not only enhance the anti-stress ability of aquatic animals but also play an important role in disease prevention and control.
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Yang, H., Zhang, Y., Wei, W. (2021). Heat Shock Proteins (Chaperones) and Role in Aquatic Animal Disease Management. In: Gupta, S.K., Giri, S.S. (eds) Biotechnological Advances in Aquaculture Health Management . Springer, Singapore. https://doi.org/10.1007/978-981-16-5195-3_17
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