Comparative Analysis of Heat Shock Protein Genes Hsp70 and Hsp90 Expression by Live and Killed Edwardsiella tarda Challenge in Rohu, Labeo rohita
Akash Jayalakshmi Subramaniyan, Kurcheti Pani Prasad, Saurav Kumar, Nalini Poojary, Anisha Valsalam and Megha Kadam Bedekar*
Aquatic Environment and Health Management Division, ICAR-Central Institute of Fisheries Education, Mumbai, India
*Corresponding Author: Megha Kadam Bedekar, Aquatic Environment and Health Management Division, ICAR-Central Institute of Fisheries Education, Mumbai, India.
October 03, 2022; Published: October 21, 2022
An inclusive variety of biotic and abiotic pressures fuels specific intracellular stress responses characterized by a family of unique proteins referred to as heat shock proteins (HSP). The present study is an expression profiling of two significant heat shock protein genes, Hsp70 and Hsp90, during live (lethal, sublethal) and killed Edwardsiella tarda challenge in rohu, Labeo rohita. Thirty rohu juveniles were challenged with the lethal dose (LD50) of E. tarda 3.5×107 CFU, the sublethal dose of E. tarda 3.5×106 CFU, and formalin-killed E. tarda 3.5×107 CFU per 20g of body weight of fish, intraperitoneally. The genes' (Hsp70 and Hsp90) expressions were studied in the liver, kidney, spleen, and gill tissues of rohu at different periods: 0, 3, 6, 12, 24, 48, and 72 hours post-challenge by qPCR. The Hsp gene modulation was more significant in the liver and spleen than in kidney and gill tissues. Among the three treatments, the killed E. tarda showed more expression of Hsp70 production followed by the lethal dose. High Hsp90 expression was observed in fishes challenged with live E. tarda than killed bacteria. Further, the highest activity of glutathione peroxidase and myeloperoxidase was found in all the treatments. The study indicated the critical role of Hsp70 and Hsp90 in live infection compared to killed bacterial administration.
Keywords: Heat Shock Proteins; HSP 70; HSP 90; Edwardsiella tarda; Labeo rohita
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