Functional characterization of peroxiredoxin 5 from yellowtail clownfish (Amphiprion clarkii): Immunological expression assessment, antioxidant activities, heavy metal detoxification, and nitrosative stress mitigation

• Published in: Developmental and comparative immunology 2025-01, Vol.162, p.105289, Article 105289
• Main Authors: Rodrigo, D.C.G., Udayantha, H.M.V., Liyanage, D.S., Omeka, W.K.M., Kodagoda, Y.K., Hanchapola, H.A.C.R., Dilshan, M.A.H., Ganepola, G.A.N.P., Warnakula, W.A.D.L.R., Kim, Gaeun, Kim, Jeongeun, Lee, Jihun, Wan, Qiang, Lee, Jehee
• Format: Article
• Language: English
• Subjects: Amphiprion clarkii; Antioxidant; Innate immune response; Oxidative stress; Peroxiredoxin 5
• ISSN: 0145-305X; 1879-0089; 1879-0089
• DOI: 10.1016/j.dci.2024.105289

Peroxiredoxin 5 (Prdx5) is the last recognized member of Prdx family. It is a unique, atypical, 2-Cys antioxidant enzyme, protecting cells from death caused by reactive oxygen species (ROS). In this study, the Prdx5 ortholog of Amphiprion clarkii (AcPrdx5) was identified and characterized to explore its specific structural features and functional properties. The open reading frame of AcPrdx5 is 573 bp long and encodes 190 amino acids containing a mitochondrial targeting sequence, thioredoxin domain, and two conserved cysteine residues responsible for antioxidant function. The predicted molecular weight and theoretical isoelectric point of AcPrdx5 are 20.3 kDa and 9.01, respectively. AcPrdx5 sequences were found to be highly conserved across the other orthologs from various organisms and it distinctively clustered within the fish Prdx5 subclade of the phylogenetic tree. The expression of AcPrdx5 was ubiquitously detected among twelve tested tissues, with the highest level in the brain. Furthermore, the mRNA levels of AcPrdx5 in the blood and head-kidney tissues were significantly (p