Presentation Is Essential for Glycan-Lectin Recognition at the Molecular and Cellular Levels: The Interaction of Tumor-Associated O‑Glycans with the Macrophage Galactose-Type Lectin.

ABSTRACT: The human macrophage galactose-type lectin (MGL) recognizes exposed GalNAc residues abundantly found in tumor O-glycans. Herein, we have used an integrative chemical, structural, and functional approach to unravel the intricate specificity and molecular determinants that underlie the recognition of Thomsen-nouveau (Tn), the sialylated variant (STn), and Thomsen-Friedenreich (TF) O-glycans by the carbohydrate recognition domain of the MGL (MGL-CRD) at the molecular and cellular levels. The MGL-CRD prefers binding to Tn > STn ≫ TF O-glycans. In this molecular context, NMR, isothermal titration calorimetry, and molecular dynamics simulations revealed quantitative key structural and dynamic differences in binding, depending on the O-glycan. Interestingly, the densit

SUBMITTER: Grosso AS 

PROVIDER: S-EPMC12848722 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature