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T.D.W. Kasthuriarachchi,J.C. Harasgama,Seongdo Lee,Hyukjae Kwon,Qiang Wan,Jehee Lee 제주대학교 해양과학연구소 2021 해양과환경연구소 연구논문집 Vol.45 No.-
β-catenin is a structural protein that makes the cell-cell connection in adherence junctions. Besides the structural functions, it also plays a role as a central transducer of the canonical Wnt signaling cascade, regulating nearly four hundred genes related to various cellular processes. Recently the immune functions of β-catenin during pathogenic invasion have gained more attention. In the present study, we elucidated the immune function of fish β-catenin by identifying and characterizing the β-catenin homolog (PhCatβ) from redlip mullet, Planiliza haematocheila. The complete open reading frame of PhCatβ consists of 2352 bp, which encodes a putative β-catenin homolog (molecular weight: 85.7 kDa). Multiple sequence alignment analysis revealed that β-catenin is highly conserved in vertebrates. Phylogenetic reconstruction demonstrated the close evolutionary relationship between PhCatβ and other fish β-catenin counterparts. The tissue distribution analysis showed the highest mRNA expression of PhCatβ in heart tissues of the redlip mullet under normal physiological conditions. While in response to pathogenic stress, the PhCatβ transcription level was dramatically increased in the spleen and gill tissues. The overexpression of PhCatβ stimulated M2 polarization and cell proliferation of murine RAW 264.7 macrophage. In fish cells, the overexpression of PhCatβ resulted in a significant upregulation of antiviral gene transcription and vice versa. Moreover, the overexpression of PhCatβ could inhibit the replication of VHSV in FHM cells. Our results strongly suggest that PhCatβ plays a role in macrophage activation and antiviral immune response in redlip mullet.
W.S.P. Madhuranga,M.D. Neranjan Tharuka,J.C. Harasgama,Hyukjae Kwon,Qiang Wan,Jehee Lee 제주대학교 해양과학연구소 2021 해양과환경연구소 연구논문집 Vol.45 No.-
Interferon-induced protein 35 kDa (IFP35) has been demonstrated to play important roles in antiviral defense, inflammatory response and cancer progression. However, its precise function in teleost fish remains to be elucidated. Herein, we functionally characterized the rock bream (Oplegnathus fasciatus) IFP35 (OfIFP35) to understand its expression pattern, subcellular localization, antiviral activity, and regulation of downstream genes. OfIFP35 consists of an 1107 bp open reading frame encoding 368 amino acids, including two N-mycinteractor (Nmi)/IFP35 domains (NIDs). The predicted molecular weight of OfIFP35 was 42 kDa, with a theoretical isoelectric point (pI) of 5.10. Evolutionary conservation of IFP35 was analyzed using multiple, pairwise alignments and phylogenetic tree analysis. OfIFP35 in rock bream was found to be highest expressed in the gills. Immune challenges with iridovirus, polyinosinic:polycytidylic acid, lipopolysaccharide, and live bacteria (Streptococcus iniae and Edwardsiella tarda) significantly upregulated its mRNA expression in gill and liver tissues of the rock bream. GFP-tagged OfIFP35 was localized in the cytoplasm of FHM cells, and its overexpression significantly suppressed VHSV transcription in vitro. Moreover, the analysis of downstream gene expression revealed that OfIFP35 could activate the type I interferon pathway. Collectively, these findings indicate that OfIFP35 is important for the immune system of rock bream as it promotes defense responses during viral infections.