Galectin-8-like isoform X1 mediates antibacterial, antiviral, and antioxidant responses in red-lip mullet (Planiliza haematocheilus) through positive modulation of pro-inflammatory cytokine, chemokine, and enzymatic antioxidant activity

Galectin 8 belongs to the tandem repeat subclass of the galectin superfamily. It possesses two homologous carbohydrate recognition domains linked by a short peptide and preferentially binds to β-galactoside-containing glycol-conjugates in a calcium-independent manner. This study identified Galectin-...

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Published in:Developmental and comparative immunology 2024-08, Vol.157, p.105182-105182, Article 105182
Main Authors: Warnakula, W.A.D.L.R., Udayantha, H.M.V., Liyanage, D.S., Tharanga, E.M.T., Omeka, W.K.M., Dilshan, M.A.H., Hanchapola, H.A.C.R., Jayasinghe, J.D.H.E., Jeong, Taehyug, Wan, Qiang, Lee, Jehee
Format: Article
Language:English
Subjects:
Animals
Antibacterial
Antioxidant
Antioxidants - metabolism
Antiviral
Antiviral Agents - metabolism
Chemokines - genetics
Chemokines - metabolism
Cytokines - metabolism
Cytokines and chemokines
Fish Diseases - immunology
Fish Proteins - genetics
Fish Proteins - immunology
Fish Proteins - metabolism
Galectin-8
Galectins - genetics
Galectins - metabolism
Immunity, Innate
Innate immunity
Lactococcus - physiology
Lipopolysaccharides - immunology
Novirhabdovirus - immunology
Novirhabdovirus - physiology
Poly I-C - immunology
Protein Isoforms - genetics
Protein Isoforms - metabolism
Smegmamorpha - genetics
Smegmamorpha - immunology
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Summary:Galectin 8 belongs to the tandem repeat subclass of the galectin superfamily. It possesses two homologous carbohydrate recognition domains linked by a short peptide and preferentially binds to β-galactoside-containing glycol-conjugates in a calcium-independent manner. This study identified Galectin-8-like isoform X1 (PhGal8X1) from red-lip mullet (Planiliza haematocheilus) and investigated its role in regulating fish immunity. The open reading frame of PhGal8X1 was 918bp, encoding a soluble protein of 305 amino acids. The protein had a theoretical isoelectric (pI) point of 7.7 and an estimated molecular weight of 34.078 kDa. PhGal8X1 was expressed in various tissues of the fish, with prominent levels in the brain, stomach, and intestine. PhGal8X1 expression was significantly (p 
ISSN:0145-305X
1879-0089
DOI:10.1016/j.dci.2024.105182