Response to Oswald et al.: ST6Gal1 in plasma is dispensable for IgG sialylation

Glycobiology. 2022 Oct 31;32(11):917-918. doi: 10.1093/glycob/cwac055.

Abstract

The presence or absence of terminal sialic acid residues in the sugar moiety attached to the Fc-domain of IgG molecules modulates IgG activity and is associated with autoimmune or infection related inflammation. In a recent paper, Oswald and colleagues suggest that IgG sialylation may occur post IgG secretion from plasma cells, which would be a major issue for therapeutic antibodies injected into patients. In contrast, we argue that previous work rather demonstrates that IgG sialylation occurs within B cells and that the experimental system used by the authors is not suitable to address this critical question.

Keywords: antibody; autoimmunity; sialic acid.

Publication types

  • Research Support, Non-U.S. Gov't
  • Comment

MeSH terms

  • Antigens, CD
  • B-Lymphocytes
  • Humans
  • Immunoglobulin G* / chemistry
  • Inflammation
  • N-Acetylneuraminic Acid*
  • Sialyltransferases / genetics

Substances

  • Immunoglobulin G
  • N-Acetylneuraminic Acid
  • ST6GAL1 protein, human
  • Sialyltransferases
  • Antigens, CD