Publication: Molecular characterization of Galectin-8 from Nile tilapia (Oreochromis niloticus Linn.) and its response to bacterial infection
1
Issued Date
2015-12-01
Resource Type
ISSN
18729142
01615890
01615890
Other identifier(s)
2-s2.0-84948967283
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Molecular Immunology. Vol.68, No.2 (2015), 585-596
Suggested Citation
Sasimanas Unajak, Nutthida Pholmanee, Napat Songtawee, Kornsorn Srikulnath, Prapansak Srisapoome, Asama Kiataramkul, Hidehiro Kondo, Ikuo Hirono, Nontawith Areechon Molecular characterization of Galectin-8 from Nile tilapia (Oreochromis niloticus Linn.) and its response to bacterial infection. Molecular Immunology. Vol.68, No.2 (2015), 585-596. doi:10.1016/j.molimm.2015.09.012 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/35340
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Molecular characterization of Galectin-8 from Nile tilapia (Oreochromis niloticus Linn.) and its response to bacterial infection
Abstract
© 2015 Elsevier Ltd. Galectins belong to the family of galactoside-binding proteins and play a major role in the immune and inflammatory responses of vertebrates and invertebrates. The galectin family is divided into three subtypes based on molecular structure; prototypes, chimera types, and tandem-repeated types. We isolated and characterized the cDNA of galectin-8 (OnGal-8) in Nile tilapia (Oreochromis niloticus). OnGal-8 consisted of a 966 bp open reading frame (ORF) that encoded a 321 amino acid protein (43.47 kDa). Homology and phylogenetic tree analysis suggested the protein was clustered with galectin-8s from other animal species and shared at least 56.8% identity with salmon galectin-8. Structurally, the amino acid sequence included two distinct N- and C- terminus carbohydrate recognition domains (CRDs) of 135 and 133 amino acids, respectively, that were connected by a 39 amino acid polypeptide linker. The N- and C-CRDs contained two conserved WG-E-I and WG-E-T motifs, suggesting they have an important role in mediating the specific interactions between OnGal-8 and saccharide moieties such as β-galactoside. The structure of OnGal-8 was characterized by a two-fold symmetric pattern of 10-and 12-stranded antiparallel ß-sheets of both N- and C-CRDs, and the peptide linker presumably formed a random coil similar to the characteristic tandem-repeat type galectin. The expression of OnGal-8 in healthy fish was highest in the skin, intestine, and brain. Experimental challenge of Nile tilapia with S. agalactiae resulted in significant up-regulation of OnGal-8 in the spleen after 5 d. Our results suggest that OnGal-8 is involved in the immune response to bacterial infection.