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Publication Abstract from PubMed

The near-germline antibody S25-2 exhibits a remarkable cross-reactivity for oligosaccharides containing the bacterial lipopolysaccharide carbohydrate 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo). The recent synthesis of a variety of Kdo analogues permits a detailed structural analysis of the importance of specific interactions in antigen recognition by S25-2. The Kdo disaccharide analogue Kdo-(2-->4)-5,6-dehydro-Kdo lacks a 5-OH group on the second Kdo residue and has been cocrystallized with S25-2. The structure reveals that the modification of the Kdo residue at position 5 results in a rearrangement of intramolecular hydrogen bonds in the antigen that allows it to assume a novel conformation in the antibody-combining site. The cross-reactive binding of S25-2 to this synthetic ligand highlights the adaptability of this antibody to non-natural synthetic analogues.

Exploring the cross-reactivity of S25-2: complex with a 5,6-dehydro-Kdo disaccharide.,Brooks CL, Wimmer K, Kosma P, Muller-Loennies S, Brade L, Brade H, Evans SV Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):2-5. doi:, 10.1107/S1744309112047422. Epub 2012 Dec 25. PMID:23295476^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.