Galectins are lectins possessing an evolutionarily conserved carbohydrate recognition domain (CRD) with affinity for β-galactoside. The key role played by innate immunity in invertebrates has recently become apparent. Herein, a… Click to show full abstract
Galectins are lectins possessing an evolutionarily conserved carbohydrate recognition domain (CRD) with affinity for β-galactoside. The key role played by innate immunity in invertebrates has recently become apparent. Herein, a full-length galectin (ScGal) was identified in razor clam (Sinonovacula constricta). The 528 bp open reading frame encodes a polypeptide of 176 amino acids with a single CRD and no signal peptide. ScGal mRNA transcripts were mainly expressed in hemolymph and gill, and were significantly up-regulated following bacterial challenge. Recombinant rScGal protein binds to and aggregates various bacteria, and has affinity for peptidoglycan, lipoteichoic acid and d-galactose. The protein also stimulates hemocytes to phagocytose invading bacterial pathogens. ScGal is an important immune factor in innate immunity, and a small protein with multiple important functions.
               
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