IgG and IgM antibodies to the refolded MOG(1-125) extracellular domain in humans

J Neuroimmunol. 2011 Apr;233(1-2):216-20. doi: 10.1016/j.jneuroim.2010.11.011. Epub 2011 Jan 7.

Abstract

Antibodies to MOG in serum have a dubious prognostic value in multiple sclerosis. The MOG recombinant protein conformational properties relevant to the antigenic activity are unknown. We employed a solid-phase ELISA based on a product (rMOG(ED)(His)(6)) expressed in E. coli after subcloning the cDNA of the extracellular domain of rat MOG, performing a refolding procedure on column and affinity purification. The far-UV Circular Dichroism (CD) spectra of rMOG(ED)(His)(6) showed a β-sheet, a characteristic feature of the Ig-fold. However, in MS sera and controls we failed to detected IgM or IgG antibodies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Animals
  • Extracellular Space / chemistry
  • Extracellular Space / immunology
  • Female
  • Humans
  • Immunoglobulin G / analysis
  • Immunoglobulin G / blood*
  • Immunoglobulin M / analysis
  • Immunoglobulin M / blood*
  • Male
  • Middle Aged
  • Multiple Sclerosis / diagnosis
  • Multiple Sclerosis / immunology*
  • Multiple Sclerosis / metabolism*
  • Myelin Proteins
  • Myelin-Associated Glycoprotein / chemistry
  • Myelin-Associated Glycoprotein / immunology*
  • Myelin-Oligodendrocyte Glycoprotein
  • Protein Folding*
  • Protein Structure, Tertiary / physiology
  • Rats
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / immunology
  • Young Adult

Substances

  • Immunoglobulin G
  • Immunoglobulin M
  • MOG protein, human
  • Mog protein, rat
  • Myelin Proteins
  • Myelin-Associated Glycoprotein
  • Myelin-Oligodendrocyte Glycoprotein
  • Recombinant Proteins