Localisation of the monocyte-binding region on human immunoglobulin G

J. M. Woof, L. J. Partridge, R. Jefferis, D. R. Burton (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

111 Citations (Scopus)

Abstract

Earlier studies, which provided indirect evidence for the involvement of the Cγ2 domain of human immunoglobulin G (IgG) in human immunoglobulin G (IgG) in human monocyte binding, have been extended to further localise the site of interaction on human IgG. A number of IgGs from several different species and fragments of human IgGs were assayed for ability to inhibit the interaction of radio-labelled human IgG and the human monocyte. By comparison of the amino-acid sequences of those IgGs found to exhibit relatively tight, intermediate or weak binding to human monocyte Fc receptors we are able to postulate a possible monocyte-binding site on human IgG. In addition, the results have implications for the applicability of monoclonal antibodies and antisera when used in the presence of human monocytes and possibly macrophages.

Original languageEnglish
Pages (from-to)319-330
Number of pages12
JournalMolecular Immunology
Volume23
Issue number3
DOIs
Publication statusPublished - Mar 1986

Keywords

  • Amino Acid Sequence
  • Animals
  • Antibody Affinity
  • Binding Sites, Antibody
  • Cattle
  • Complement Activating Enzymes/immunology
  • Complement C1q
  • Goats
  • Guinea Pigs
  • Hot Temperature
  • Humans
  • Immunoglobulin G/immunology
  • Mice
  • Monocytes/immunology
  • Rats
  • Receptors, Fc/immunology
  • Sheep
  • Swine

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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