The role of three heat shock protein genes in the immune response to Aeromonas hydrophila challenge in marbled eel, Anguilla marmorata

Abstract

Heat shock proteins (HSPs) are highly conserved molecular chaperones that play critical roles in both innate and adaptive immunity. However, little information about HSPs from marbled eel Anguilla marmorata is known. In this study, the full-length Amhsp90 (2527 bp), Amhsp70 (2443 bp) and Amhsc70 (2247 bp) were first cloned from A. marmorata, using rapid amplification of cDNA ends, containing open reading frames of 2181, 1932 and 1950 bp in length, and encoding proteins with 726, 643 and 649 amino acids, respectively. The deduced amino acid sequences of three Amhsps shared a high homology similarity with other migratory fish. Real-time fluorescent quantitative polymerase chain reaction was used to evaluate tissue-specific distribution and mRNA expression levels of three Amhsps subjected to infection with Aeromonas hydrophila. The mRNA expression of three Amhsps in eight tested tissues, namely liver, heart, muscle, gill, spleen, kidney, brain and intestine, of juvenile A. marmorata was evaluated to reveal the major expression distribution in liver, intestine, muscle and heart. After pathogen challenge treatments, mRNA transcriptions of three Amhsps revealed a significant regulation at various time points in the same tissue. All these findings suggest that Amhsps may be involved in the immune response in A. marmorata.

Thermal Stress of Ambient Temperature Modulate Expression of Stress and Immune-Related Genes and Dna Fragmentation in Nile Tilapia (Oreochromis Niloticus (Linnaeus, 1758))

“…Wang et al (2007) observed its up-regulation among HSPs expressed in summer in goldfish and its expression was higher in gills than liver. We also observed that its summer level of expression is higher than winter but liver level exceed gills which may be attributed to species difference in regulatory roles of HSPs (Liang et al, 2016).…”

Exploring bacterial community composition and immune gene expression of European eel larvae (Anguilla anguilla) in relation to first-feeding diets

“…Generally, heat shock proteins are constitutively expressed in cells to maintain a number of critical cellular processes relating to protein folding, fidelity and translocation with the task to ensure survival by protecting vital cellular functions [ 67 ]. As such, this family of proteins is also commonly referred to as “stress/repair proteins” and an upregulation of hsp90 has been previously described in several fish species, including the responses of silver sea bream ( Sparus sarba ) to Vibrio alginolyticus [ 68 ], miiuy croaker ( Miichthys miiuy ) to Vibrio anguillarum [ 69 ], and marbled eel ( Anguilla marmorata ) to Aeromonas hydrophila [ 70 ]. Thus, in the present study, the upregulation of hsp90 observed on 22 dph, might be a response to the presence of potentially harmful bacteria in the larval bacterial community, triggering the activation of the stress/repair mechanism, which might be of key essence, especially considering that the larval immunocompetence is not yet fully developed.…”