Molecular importance of prawn large heat shock proteins 60, 70 and 90

Abstract

Considering the importance of heat shock proteins (HSPs) in the innate immune system of prawn, a comparative molecular approach was proposed to study the crustacean large HSPs 60, 70 and 90. Three different large HSPs were identified from freshwater prawn Macrobrachium rosenbergii (Mr) cDNA library during screening. The structural and functional characteristic features of HSPs were studied using various bioinformatics tools. Also, their gene expression and mRNA regulation upon various pathogenic infections was studied by relative quantification using 2-ΔΔCT method. MrHSP60 contains a long chaperonin 60 domain at 46-547 which carries a chaperonin 60 signature motif between 427 and 438, whereas MrHSP70 contains a long HSP70 domain at 21-624 and MrHSP90 carries a HSP90 domain at 188-719. The two dimensional analysis showed that MrHSP60 contains more amino acids (52%) in helices, whereas MrHSP70 (40.6%) and MrHSP90 (51.8%) carried more residues in coils. Gene expression results showed significant (P < 0.05) expression of MrHSP60, 70 and 90 in haemocyte, gill and hepatopancreas, respectively. Further, the expression level was up-regulated upon bacterial (Aeromonas hydrophilla and Vibrio harveyi) and viral [white spot syndrome virus (WSSV) and M. rosenbergii nodo virus (MrNV)] infections during various time periods. The gene expression results exhibited the potential involvement of these three HSPs in the immune system of prawn. The study indicated the potentiality of these molecules, thereby protecting cells against pathogens as well as severe cellular and environmental stresses in crustaceans.

Impacts of environmental and biological stressors on immune system ofMacrobrachium rosenbergii

“…Three more cDNA sequences encoding heat shock proteins such as HSP60 (HG001456), HSP70 (HG001455) and HSP90 (HG001457) were also identified from M. rosenbergii cDNA library (Chaurasia et al . ).…”

“…; Chaurasia et al . b), anti‐lipopolysaccharide factor (Arockiaraj et al . ) and lectin (Arockiaraj et al .…”

Molecular cloning of heat shock protein 60 from Marsupenaeus japonicus and its expression profiles at early developmental stages and response to heat stress

“…In the previous studies, MjHSP60 was found to be mainly expressed in defence and digestive tissues including the hepatopancreas, haemocytes, gills and the stomach, which are in direct contact with the external environment and are more vulnerable to invading pathogens and exogenous compounds (Chaurasia et al., ; Yang et al., ; Zhou, Wang, He, et al., ; Zhou, Wang, Xin, et al., ). In our study, MjHSP60 was ubiquitously expressed in all examined tissues of M .…”

“…HSP60 is a major node in the intracellular chaperone network and plays a crucial role in stress response, especially in heat stress (Chaurasia et al., ; Quintana & Cohen, ; Shi et al., ; Xu et al., ; Xu & Qin, ; Yang et al., ; Zhou, Wang, Xin, et al., ). In this study, the expression level of MjHSP60 in both gills and hepatopancreas of M .…”

“…HSPs are categorized into several families, including HSP110, Hsp100, HSP 90, HSP70, HSP 60 and the small HSPs (sHSPs), according to their sequence homology and molecular mass (Feder & Hofmann, ). Among the heat shock protein family, HSP60 plays an important role in the protein‐folding system and is capable of responding to various stressors (Chaurasia et al., ; Shi et al., ; Xu & Qin, ; Xu et al., ; Yang et al., ; Zhou, Wang, Xin, et al., ). Several HSP60 from shrimps were recently identified and characterized (Shi et al., ; Zhou, Wang, He, et al., ).…”