Recognition of Lewis X by Anti-Le x Monoclonal Antibody IG5F6

作者: Sinthuja Jegatheeswaran , France-Isabelle Auzanneau

DOI: 10.4049/JIMMUNOL.1900806

关键词: AntibodyMonoclonal antibodyBinding siteChemistryResidue (chemistry)Stereochemistry

摘要: mAbs directed toward the Lewis X (Lex) determinant have been shown to display different specificities, depending on presentation of Lex immune system. Of interest is murine anti-Lex mAb IG5F6, generated against O chain polysaccharide Helicobacter pylori that contains polymeric structures. The was found a higher affinity for over monomeric In this study, we explore recognition by IG5F6 using panel analogues in which N-acetyl-d-glucosamine, l-fucose, or d-galactose (D-Gal) are replaced with d-glucose and/or l-rhamnose. Our studies show all were weaker inhibitors than Ag, indicating three residues essential IG5F6. We explored involvement 4″-OH d-Gal binding 4″-modified analogues. Although only involved weak polar interaction, conclude D-Gal residue primarily aromatic stacking interactions Ab site. compared these results our work SH1. between and an also suggested SH1, H-bond involving identified not Thus, SH1 bind manners, even though hydrophobic patch displayed β-galactoside both cases their Lex.

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