STD-NMR Used To Elucidate the Fine Binding Specificity of Pathogenic Anti-Ganglioside Antibodies Directly in Patient Serum

RS Houliston, B.C. Jacobs, Anne Gillen, JJ Verschuuren, NH Khieu, M Gilbert, HC Jarrell

Research output: Contribution to journalArticleAcademicpeer-review

12 Citations (Scopus)

Abstract

High-resolution binding profiles were elucidated for anti-GM I IgM autoantibodies from two patients with a progressive form of paraproteinemic polyneuropathy. Antibody-ligand interaction was characterized by generating STD-NMR signals in target ganglio-oligosaccharides added directly to patient sera, without the requirement of antibody fractionation. Both immunoglobulins were found to have similar binding modalities, with interaction confined to two distinct spatially separated regions of GM1: the terminal beta Gal(1-3)beta GalNAc disaccharide unit and the sialic acid residue. We describe a unique and powerful biophysical technique applied to define the molecular interaction between autoimmune disease-causing antibodies and their ganglioside targets.
Original languageUndefined/Unknown
Pages (from-to)220-222
Number of pages3
JournalBiochemistry
Volume48
Issue number2
DOIs
Publication statusPublished - 2009

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