Monoclonal IgM from patients with peripheral demyelinating neuropathies cross‐react with bacterial polypeptides

  title={Monoclonal IgM from patients with peripheral demyelinating neuropathies cross‐react with bacterial polypeptides},
  author={Jean Claude Brouet and Xavier Mariette and M. C. Gendron and M L Dubreuil},
  journal={Clinical \& Experimental Immunology},
Human monoclonal IgM associated with a demyelinating peripheral neuropathy often feature a distinct antibody activity directed against a glucuronyl sulphate epitope shared by myelin‐associated glycoprotein (MAG), nerve glycolipids and low molecular weight peripheral nerve polypeptides‐ Earlier studies showed that these IgM use a diverse repertoire of VH, and VL genes which exhibit somatic mutations, possibly indicative of an antigen‐driven process. Here, we investigated whether such monoclonal… 
Autoantibodies associated with peripheral neuropathy
The origins of the antibodies, evidence for and against their involvement in pathogenic mechanisms, and the implications of these findings for therapy are discussed.
Myelin protein P0‐specific IgM producing monoclonal B cell lines were established from polyneuropathy patients with monoclonal gammopathy of undetermined significance (MGUS)
The immunomagnetic selection technique was successfully used for isolation of antimyelin protein P0‐specific clones, which may provide useful tools in studies of monoclonal gammopathies, leukaemia, and autoimmune diseases, including aspects of antigen‐presentation by these cells followed by T cell activation.
Cytomegalovirus is not associated with IgM anti–myelin‐associated glycoprotein/sulphate‐3‐glucuronyl paragloboside antibody–associated neuropathy
No evidence of an association between CMV infection and anti‐MAG/SGPG antibodies associated with paraproteinemic peripheral neuropathy is reported.
Immunoglobulin gene analysis in polyneuropathy associated with IgM monoclonal gammopathy
Myelin protein zero is naturally processed in the B cells of monoclonal gammopathy of undetermined significance of immunoglobulin M isotype: aberrant triggering of a patient’s T cells
It is shown for the first time that myelin protein zero is naturally processed in B cells from monoclonal gammopathy of undetermined significance, acting as aberrant antigen-presenting cells in activation of a patient’s T helper cells.
Antibody testing in peripheral nerve disorders.
Correlation between cytomegalovirus infection and IgM anti‐MAG/SGPG antibody–associated neuropathy
The strong correlation of anti‐MAG/SGPG–positive CP with the presence of serum CMV DNA suggests that CMV infection induces the IgM anti‐ MAG/ SGPG antibody.
Serum autoantibodies to neurofilament proteins in sporadic amyotrophic lateral sclerosis


Myelin‐Associated Glycoprotein Is the Antigen for a Monoclonal IgM in Polyneuropathy
It is demonstrated that the antigen for this antibody is a specific glycop protein component of myelin, referred to as myelin‐associated glycoprotein (MAG), which cross‐reacted with MAG from bovine CNS, but not from rabbit, rat, or mouse.
Complement-mediated demyelination in patients with IgM monoclonal gammopathy and polyneuropathy.
Demyelination in polyneuropathy associated with IgM monoclonal gammopathy may be mediated by complement, and alterations in myelin geometry caused by the separation of myelin lamellae corresponded to sites at which terminal-complement complex was deposited.
Reactivity of human monoclonal IgM with nerve glycosphingolipids
Sera from patients with neuropathy and monoclonal IgM, with or without antibody activity to myelin‐associated glycoprotein (MAG), as well as sera from non‐neurologic patients with Waldenström's macroglobulinaemia, with various nerve glycolipids extracts or with purified gangliosides are examined.
IgM in a human neuropathy related to paraproteinemia binds to a carbohydrate determinant in the myelin-associated glycoprotein and to a ganglioside.
  • A. A. Ilyas, R. Quarles, R. Brady
  • Biology, Medicine
    Proceedings of the National Academy of Sciences of the United States of America
  • 1984
The results indicate that the IgM paraproteins in patients with paraproteinemia and peripheral neuropathy react with a carbohydrate determinant that is shared between MAG and a peripheral nerve ganglioside.
Plasma cell dyscrasia and peripheral neuropathy: identification of the myelin antigens that react with human paraproteins.
Immunostaining was specific for the paraprotein light chain type, and absorption of the patients' sera with human peripheral nerve myelin eliminated the reaction with the central nervous system proteins.
Experimental demyelination of nerve induced by serum of patients with neuropathy and an anti‐MAG IgM M‐protein
Demyelination of feline sciatic nerve was induced by intraneural injection of serum from three patients with neuropathy and an IgM M- protein that reacted with myelin-associated glycoprotein (MAG), and deposition of the injected M-protein and complement on the surface of myelin sheaths demonstrated.
Expression of a public idiotype by human monoclonal IgM directed to myelin-associated glycoprotein and characterization of the variability subgroup of their heavy and light chains
Partial aminoterminal sequence of heavy and light chains showed that anti-MAG IgM use either lambda chains or kappa light chains of different variability subgroups, which distinguish these IgM from other human monoclonal IgM with a defined antibody activity, such as rheumatoid factors or cold agglutinins.
Nucleotidic sequence analysis of the variable domains of four human monoclonal IgM with an antibody activity to myelin‐associated glycoprotein
We determined the nucleotide sequence of the VL and VH regions of four human monoclonal IgM directed to myelin‐associated glycoprotein (MAG) and a nerve glycolipid, the sulfated glucuronic
H chain V region sequences of three human monoclonal IgM with anti-myelin-associated glycoprotein activity.
These data, together with results obtained from the sequence of the three kappa L chains of the same IgM molecules, indicate that the repertoire of VL and VH gene segments used by anti-MAG IgM is quite diverse, in contrast to previous structural data obtained for other human monoclonal IgM autoantibodies.