Complement-immunoglobulin interactions.

Journal Article (Review)

Normal circulating immunoglobulin may control complement binding to targets and thereby the manifestations of autoimmune disease. Molecular analysis of IgG and IgM mutants suggests that C1q binding by IgG utilizes a core Glu-X-Lys-X-Lys motif (where X is any amino acid). Additional amino acids, particularly homologous proline residues at position 331 in IgG and 436 in IgM, appear critical for classical pathway initiation. Glycosylation of IgG heavy chain is important in C1q binding, as well as glycosylation of IgA heavy chain for alternative pathway initiation. Additional recent evidence suggests an important role for C3 in antigen presentation. The data also raise the possibility that C3 plays a significant role in the intracellular antigen processing pathway.

Full Text

Duke Authors

Cited Authors

  • Miletic, VD; Frank, MM

Published Date

  • February 1995

Published In

Volume / Issue

  • 7 / 1

Start / End Page

  • 41 - 47

PubMed ID

  • 7772281

International Standard Serial Number (ISSN)

  • 0952-7915

Language

  • eng

Conference Location

  • England