Full-length galectin-8 and separate carbohydrate recognition domains: the whole is greater than the sum of its parts?

CAGNONI AJ; MARIÑO KV; TRONCOSO MF; ELOLA MT; RABINOVICH GA

BIOCHEMICAL SOCIETY TRANSACTIONS

PORTLAND PRESS LTD

Lugar: Londres; Año: 2020 vol. 48 p. 1255 - 1268

0300-5127

Galectin-8 (Gal-8) is a tandem-repeat type galectin with affinity for β-galactosides,bearing two carbohydrate recognition domains (CRD) connected by a linker peptide. TheN- and C-terminal domains (Gal-8N and Gal-8C) share 35% homology, and their glycanligand specificity is notably dissimilar: while Gal-8N shows strong affinity for α(2-3)-sialylatedoligosaccharides, Gal-8C has higher affinity for non-sialylated oligosaccharides,including poly-N-acetyllactosamine and/ or A and B blood group structures. Particularlyrelevant for understanding the biological role of this lectin, full-length Gal-8 can bind cellsurface glycoconjugates with broader affinity than the isolated Gal-8N and Gal-8Cdomains, a trait also described for other tandem-repeat galectins. Herein, we aim todiscuss the potential use of separate CRDs in modelling tandem-repeat galectin-8 and itsbiological functions. For this purpose, we will cover several aspects of the structure?functionrelationship of this protein including crystallographic structures, glycan specificity,cell function and biological roles, with the ultimate goal of understanding the potentialrole of each CRD in predicting full-length Gal-8 involvement in relevant biologicalprocesses.