Peroxiredoxin 1 is a member of the typical 2-Cys
peroxiredoxin family, which serves diverse functions in gene expression, immune and inflammatory responses, and
tumor progression. In this study, we aimed to analyze the structural, functional, and immunomodulatory properties of
peroxiredoxin 1 from Epinephelus akaara (EaPrx1). The open reading frame of EaPrx1 is 597 base pairs in length, encoding 198
amino acids, with a molecular weight of approximately 22 kDa. The in silico analysis revealed that EaPrx1 shares a conserved
thioredoxin fold and signature motifs that are critical for its catalytic activity and oligomerization. Further, EaPrx1 is closely related to Epinephelus lanceolatus Prx1 and clustered in the Fishes group of the vertebrate clade, revealing that EaPrx1 was conserved throughout evolution. In terms of tissue distribution, a high level of EaPrx1 expression was observed in the spleen, brain, and blood tissues. Likewise, in immune challenge experiments, significant transcriptional modulations of EaPrx1 upon
lipopolysaccharide,
polyinosinic:polycytidylic acid, and nervous
necrosis virus
injections were noted at different time points, indicating the immunological role of EaPrx1 against pathogenic
infections. In the functional analysis, rEaPrx1 exhibited substantial
DNA protection,
insulin disulfide reduction, and tissue repair activities, which were concentration-dependent. EaPrx1/pcDNA™ 3.1 (+)-transfected fathead minnow cells revealed high cell viability upon
arsenic toxicity, indicating the
heavy metal detoxification activity of EaPrx1. Taken together, the transcriptional and functional studies imply critical roles of EaPrx1 in innate immunity, redox regulation, apoptosis, and tissue-repair processes in E. akaara.