Dissecting the molecular mechanism of IVIg therapy: the interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain.

@article{Yu2013DissectingTM,
  title={Dissecting the molecular mechanism of IVIg therapy: the interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain.},
  author={Xiaojie Yu and Sne{\vz}ana Vasiljevi{\'c} and Daniel A. Mitchell and Max Crispin and Christopher N. Scanlan},
  journal={Journal of molecular biology},
  year={2013},
  volume={425 8},
  pages={1253-8}
}
Intravenous immunoglobulin (IVIg) therapy is used to treat a wide range of autoimmune conditions and consists of pooled immunoglobulin G (IgG) from healthy donors. The immunosuppressive effects of IVIg are, in part, attributed to terminal α2,6-linked sialic acid residues on the N-linked glycans of the IgG Fc (fragment crystallizable) domain. This α2,6-sialylated Fc (sFc) has been reported to bind to the carbohydrate recognition domain (CRD) of the cell-surface lectin DC-SIGN (dendritic cell… CONTINUE READING