Low amounts of bisecting glycans characterize cerebrospinal fluid-borne IgG

J Neuroimmunol. 2018 Jul 15:320:19-24. doi: 10.1016/j.jneuroim.2018.04.010. Epub 2018 Apr 16.


Immunoglobulin G (IgG) harbors a conserved N-glycosylation site which is important for its effector functions. Changes in glycosylation of IgG occur in many autoimmune diseases but also in physiological conditions. Therefore, the glycosylation pattern of serum IgG is well characterized. However, limited data is available on the glycosylation pattern of IgG in cerebrospinal fluid (CSF) compared to serum. Here, we report significantly reduced levels of bisected glycans in CSF IgG. Galactosylation and sialylation of IgG4 also differed significantly. Therefore, we propose a common mechanism mediating glycosylation changes of IgG at the transition from serum to CSF in steady state conditions.

Keywords: Bisecting; Cerebrospinal fluid; Glycosylation; Immunoglobulin G; Serum; Sialylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Aged, 80 and over
  • Female
  • Glycosylation
  • Humans
  • Immunoglobulin G / blood*
  • Immunoglobulin G / cerebrospinal fluid*
  • Immunoglobulin G / chemistry*
  • Male
  • Middle Aged
  • Polysaccharides / analysis
  • Polysaccharides / chemistry


  • Immunoglobulin G
  • Polysaccharides