STD-NMR used to elucidate the fine binding specificity of pathogenic anti-ganglioside antibodies directly in patient serum: Biochemistry

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DOIResolve DOI: http://doi.org/10.1021/bi802100u
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TypeArticle
Journal titleBiochemistry
Volume48
Issue2
Pages220222; # of pages: 3
SubjectACID; Antibodies; Antibodies,Anti-Idiotypic; antibody; Autoantibodies; binding; Biophysical Processes; Blood; Canada; diagnosis; DISACCHARIDE; Enzyme-Linked Immunosorbent Assay; epitope; Epitope Mapping; Epitopes; Form; Fractionation; GANGLIOSIDE; Gangliosides; HIGH-RESOLUTION; Humans; IgM; Immunoglobulins; immunology; interaction; LIGAND; Ligands; Methods; Models,Molecular; MOLECULAR; Nuclear Magnetic Resonance,Biomolecular; Polyneuropathies; REGION; Sensitivity and Specificity; Serum; SIALIC; SIALIC-ACID; SIGNALS; SPECIFICITY; TARGET; technique; UNIT
AbstractHigh-resolution binding profiles were elucidated for anti-GM1 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 betaGal(1-3)betaGalNAc 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
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedYes
NRC numberHOULISTON2009
NPARC number9359763
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Record identifieredc83d6f-8b9a-41f5-af67-d59b35b94579
Record created2009-07-10
Record modified2016-05-09
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