Heterologous expression of newly identified galectin-8 from sea urchin embryos produces recombinant protein with lactose binding specificity and anti-adhesive activity

摘要: Galectin family members specifically bind beta-galactoside derivatives and are involved in different cellular events, including cell communication, signalling, apoptosis, immune responses. Here, we report a tandem-repeat type galectin from the Paracentrotus lividus sea urchin embryo, referred to as Pl-GAL-8. The 933nt sequence encodes protein of 34.73 kDa, containing conserved HFNPRF WGxExR motifs two highly similar carbohydrate-recognition domains (CRD). three-dimensional structure model N-CRD confirms high evolutionary conservation carbohydrate binding sites. temporal gene expression is regulated during development transcripts localize at tip archenteron gastrula stage, subset secondary mesenchyme cells that differentiate into blastocoelar (immune) cells. Functional studies using recombinant Pl-GAL-8 expressed bacteria demonstrate its hemo-agglutinating activity on human red blood through lactose, well ability inhibiting adhesion Hep-G2 substrate. recent implications autoimmune diseases inflammatory disorders make Gal-8 an attractive candidate for therapeutic purposes. Our results offer solid basis addressing use new functional applicative studies, respectively developmental biomedical fields.