The human macrophage galactose‐type lectin, MGL, recognizes the outer core of E. coli lipooligosaccharide

Carbohydrate-lectin interactions intervene in and mediate most biological processes, including a crucial modulation of immune responses to pathogens. Despite the growing interest in investigating the association between host receptor lectins and exogenous glycan ligands, the molecular mechanisms underlying bacterial recognition by human lectins are still not fully understood. Here we describe a novel molecular interaction between the human macrophage galactose-type lectin (MGL) and the lipooligosaccharide (LOS) of E. coli strain R1. Saturation Transfer Difference (STD) NMR analysis, supported by computational studies, demonstrated that MGL bound to the purified deacylated LOSR1 mainly through the recognition of its outer core and established crucial interactions with the terminal Galα(1,2)Gal epitope. These results assess the ability of MGL to recognize glycan moieties exposed on Gram-negative bacterial surfaces.