High-affinity binding of bioactive glycosylation-inhibiting factor to antigen-primed T cells and natural killer cells

Katsuji Sugie, Tatsumi Nakano, Takafumi Tomura, Kenji Takakura, Toshifumi Mikayama, Kimishige Ishizaka

Research output: Contribution to journalArticle

Abstract

High-affinity binding was demonstrated between suppressor-T-cell- derived bioactive glycosylation-inhibiting factor (GIF) and helper T hybridomas and natural killer cell line cells. Inactive GIF present in cytosol of suppressor T cells and Escherichia coli-derived recombinant human GIF (rhGIF) failed to bind to these cells. However, affinity of rhGIF for the target cells was generated by replacement of Cys-57 in the sequence with Ala or of Asn-106 with Ser or binding of 5-thio-2-nitrobenzoic acid to Cys-60 in the molecule. Such mutations and the chemical modification of rhGIF synergistically increased the affinity of GIF molecules for the target cells. The results indicated that receptors on the target cells recognize conformational structures of bioactive GIF. Equilibrium dissociation constant (K(d)) of the specific binding between bioactive rGIF derivatives and high- affinity receptors was 10-100 pM. Receptors for bioactive GIF derivatives were detected on Th1 and Th2 T helper clones and natural killer NK1.1+ cells in normal spleen but not on naive T or B cells. Neither the inactive rGIF nor bioactive rGIF derivatives bound to macrophage and monocyte lines or induced macrophages for tumor necrosis factor α production.

Original languageEnglish (US)
Pages (from-to)5278-5283
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number10
DOIs
StatePublished - May 13 1997

Keywords

  • conformational structure
  • macrophage migration inhibitory factor
  • suppressor T cells

ASJC Scopus subject areas

  • General

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