Recombinant Fc of human lgG1 prepared in an escherichia coli system escapes recognition by macrophages

Masato Nose, Ryo Takano, Satoshi Nakamura, Yoji Arata, Masahisa Kyogoku

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

The Fc portion of IgG is recognized by macrophages via Fc receptors on their cell surface. The recognition of human lgG1-Fc by macrophages was compared for the native and recomblnant proteins by a novel assay method using competitive inhibition of the aggregated IgG-medlated chemllumlnescence reaction of human macrophage cell line THP-1. Recombinant Fc proteins, prepared in an Escherichia coll system, which lack ollgosaccharides and retain normal staphylococcal protein A reactivity and, to a lesser extent, C1q binding capacity, showed Inhibitory ability >500 times lower than that of native Fc fragments obtained by proteolytlc digestion of myeloma proteins. This suggests that the oligosaccharlde chains on lgG1-Fc molecules may be critical for recognition by Fc receptors on macrophages.

Original languageEnglish
Pages (from-to)1109-1112
Number of pages4
JournalInternational immunology
Volume2
Issue number11
DOIs
Publication statusPublished - 1990 Nov

Keywords

  • Chemiluminescence
  • Fc receptor
  • N-hnked oligosacchandes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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