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Binding of immunoglobulin G antibodies in Guillain–Barré syndrome sera to a mixture of GM1 and a phospholipid: Possible clinical implications
Author(s) -
Kusunoki Susumu,
Morita Daiji,
Ohminami Shinya,
Hitoshi Seiji,
Kanazawa Ichiro
Publication year - 2003
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.10307
Subject(s) - antibody , guillain barre syndrome , immunoglobulin g , immunoglobulin m , multifocal motor neuropathy , antiserum , pathogenesis , immunology , epitope , ganglioside , medicine , chemistry , biochemistry , mismatch negativity , electroencephalography , psychiatry
Anti‐GM1 immunoglobulin G (IgG) antibodies are frequently present in sera from patients with Guillain–Barré syndrome (GBS). A previous report on a patient who had a neuropathy with immunoglobulin M (IgM) M‐protein binding to a conformational epitope formed by phosphatidic acid (PA) and gangliosides prompted us to investigate the binding of IgG antibodies in GBS sera to a mixture of GM1 and PA (GM1/PA). Of 121 GBS patients, 32 had anti‐GM1 IgG antibodies. All 32 also had antibody activity against GM1/PA. Twenty‐five (78%) of 32 patients had greater activity against GM1/PA than against GM1 alone. Twelve patients who had no anti‐GM1 IgG antibodies had IgG antibody activity against GM1/PA. No GBS patient had IgG antibody against PA alone. In contrast, two rabbit anti‐GM1 antisera had greater activity against GM1 alone than against GM1/PA. IgG antibody with greater binding activity against a mixture of GM1 and a phospholipid than against GM1 alone may have an important role in the pathogenesis of GBS and has implications for diagnosis. Muscle Nerve 27: 302–306, 2003