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Updated: Feb 4, 2026

Complementation of Splicing Activity by a Galectin-3 - U1 snRNP Complex on Beads
Published on: December 9, 2020
Expression profiling and functional characterization of galectin-3 of turbot (Scophthalmus maximus L.) in host
Mengyu Tian1, Ning Yang1, Lu Zhang1
1Marine Science and Engineering College, Qingdao Agricultural University, Qingdao, 266109, PR China.
Galectins, a family of evolutionary conserved β-galactoside-binding proteins, have been characterized in a wide range of species. Galectin-3 is the only member in the chimera type, which is a monomeric lectin with one CRD domain. A growing body of evidence have indicated vital roles of galectin-3 in innate immune responses against infection. Here, one galectin-3 gene was captured in turbot (SmLgals3) with a 1203 bp open reading frame (ORF). In comparison to other species, SmLgals3 showed the highest similarity and identity to large yellow croaker and medaka, respectively. The genomic structure analysis showed that SmLgals3 had 5 exons similar to other vertebrate species. The syntenic analysis revealed that galectin-3 had the same neighboring genes across all the selected species, which suggested the synteny encompassing galectin-3 region during vertebrate evolution. Subsequently, SmLgals3 was widely expressed in all the examined tissues, with the highest expression level in brain and the lowest expression level in skin. In addition, SmLgals3 was significantly down-regulated in intestine following both Gram-negative bacteria Vibrio anguillarum, and Gram-positive bacteria Streptococcus iniae immersion challenge. Finally, the rSmLgals3 showed strong binding ability to all the examined microbial ligands. Taken together, our results suggested SmLgals3 played vital roles in fish innate immune responses against infection. However, the knowledge of SmLgals3 are still limited in teleost species, further studies should be carried out to better characterize its detailed roles in teleost mucosal immunity.
Galectins, a family of evolutionary conserved β-galactoside-binding proteins, have been characterized in a wide range of species. Galectin-3 is the only member in the chimera type, which is a monomeric lectin with one CRD domain. A growing body of evidence have indicated vital roles of galectin-3 in innate immune responses against infection. Here, one galectin-3 gene was captured in turbot (SmLgals3) with a 1203 bp open reading frame (ORF). In comparison to other species, SmLgals3 showed the highest similarity and identity to large yellow croaker and medaka, respectively. The genomic structure analysis showed that SmLgals3 had 5 exons similar to other vertebrate species. The syntenic analysis revealed that galectin-3 had the same neighboring genes across all the selected species, which suggested the synteny encompassing galectin-3 region during vertebrate evolution. Subsequently, SmLgals3 was widely expressed in all the examined tissues, with the highest expression level in brain and the lowest expression level in skin. In addition, SmLgals3 was significantly down-regulated in intestine following both Gram-negative bacteria Vibrio anguillarum, and Gram-positive bacteria Streptococcus iniae immersion challenge. Finally, the rSmLgals3 showed strong binding ability to all the examined microbial ligands. Taken together, our results suggested SmLgals3 played vital roles in fish innate immune responses against infection. However, the knowledge of SmLgals3 are still limited in teleost species, further studies should be carried out to better characterize its detailed roles in teleost mucosal immunity.
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