Abstract
The potent multifunctionality of human galectins is based on their modular structure in a not yet fully understood manner. A strategy to dissect the contributions of individual sequence stretches to lectin activity is based on engineering variants of the natural proteins, which are composed of novel combinations of distinct parts. On proof-of-principle level, we here describe the design of a hybrid constituted by the N-terminal tail of chimera-type galectin-3 and the Nterminal carbohydrate recognition domain of tandem-repeat-type galectin-8, its production, purification and its serine phosphorylation characteristic for galectin- 3’s tail. As measured for the respective parental proteins, its binding to (neo)glycoproteins is specific for β-galactosides and inhibitable by lactose, with KD-value closer to galectin-8 than galectin-3. Cell surface staining indicated similarity of the hybrid’s reactivity to O-glycans and sensitivity for sialylation to respective properties of tandem-repeattype galectin-8 and its N-terminal domain. Applied as histochemical tool on tissue sections of murine jejunum and epididymis, intense lactose-inhibitable signals were recorded intracellularly, with a distribution profile akin to that of galectin-3. Tested as agglutinin, the hybrid was potent, excelling wild-type control galectins. The chimera-type design can thus serve as platform for tuning crosslinking activity.
Keywords: Agglutinin, glycosylation, lectin, phosphorylation, sialylation.
Graphical Abstract
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