High-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-oligosac-charides 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 βGal(1-3) βGalNAc disaccharide unit and the sialic acid residue. We describe a nique and powerful biophysical technique applied to efine the molecular interaction between autoimmune isease-causing antibodies and their ganglioside targets.

doi.org/10.1021/bi802100u, hdl.handle.net/1765/32668
Erasmus MC: University Medical Center Rotterdam

Houliston, S., Jacobs, B., Tio-Gillen, A., Verschuuren, J., Khieu, N., Gilbert, M., & Jarrell, H. (2009). STD-NMR used to elucidate the fine binding specificity of pathogenic anti-ganglioside antibodies directly in patient serum. Biochemistry, 48(2), 220–222. doi:10.1021/bi802100u