Molecular characterization of heat shock protein 70 and 90 genes and their expression analysis in air-breathing magur catfish (Clarias magur) while exposed to zinc oxide nanoparticles.

The air-breathing magur catfish (Clarias magur) are frequently challenged with high environmental pollutants, including that of various metal nanoparticles (NPs) in their natural habitats. Heat shock proteins (HSPs) are essential molecular chaperones for preserving intracellular protein homeostasis in eukaryotic cells. In aquatic animals, HSPs are known to play important defensive roles associated with various environmental stress-related cellular damages. In the present investigation, we characterized the molecular and structural organization of distinct HSPs and their potential induction of HSP genes in multiple magur catfish tissues while exposed to ZnO NPs for 14 days. The sequence alignment of four HSP genes (hsp70, hsc70, hsp90a, and hsp90b) of magur catfish demonstrated evolutionary parallels with bony fishes and total conservation of active sites across the amphibia, fish, and mammals. From the architectural analysis of HSP70, HSC70, HSP90a, and HSP90b proteins, a structural similarity with mammals was observed, suggesting the functional resemblances of the studied HSPs in chaperone mechanisms. In the examined tissues, the mRNAs of HSP genes expressed constitutively. Exposure of C. magur to ZnO NPs (10 mg/L) in situ led to a considerable increase in the levels of mRNAs for several HSP genes and translated proteins, with HSP70 exhibiting the highest level of expression. Thus, it can be contemplated that HSPs may be involved in defending the magur catfish against the ZnO NP- and other metal NP-mediated cellular damages. The results provide new insights into the involvement of HSP machinery during adaptation to the ZnO NP-induced stress in magur catfish.