Antiidiotypic antibodies mimic molecular and functional properties of human IL-1β in vitro and in vivo

E. Soprana, E. Vigo, A. Verani, J. Blom, A. G. Siccardi, D. Vercelli, G. Viale

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

We obtained affinity-purified polyclonal anti-id antibodies against mAb MhC1 and BrhC3, which recognize amino acids 133-147 at the N-terminus of mature human IL-1β. mAb MhC1 and BrhC3 have been shown to inhibit binding of IL-1β to type I IL-1R, and to neutralize IL-1β bioactivity in a number of in vitro assays. We show that affinity-purified antibodies against the MhC1 and BrhC3 idiotypes specifically bind to type I IL-1β IL-1R and that this binding is inhibited by both IL-1β and IL-1ra; anti-id antibodies were also able to trigger IL-1R-dependent events, such as IL-8 secretion by human skin fibroblasts and pyrogenic effect after injection in mice. These anti-id antibodies, therefore, behave as structural and functional 'images' of IL- 1β, both in vivo and in vitro. These data indicate the idiotypic strategy as a powerful tool to study the fine specificity of receptor-ligand interactions. Moreover, this is, to our knowledge, the first report showing that the 'internal image' of a cytokine can be active in vivo.

Original languageEnglish (US)
Pages (from-to)325-330
Number of pages6
JournalLymphokine and Cytokine Research
Volume13
Issue number5
StatePublished - Jan 1 1994
Externally publishedYes

ASJC Scopus subject areas

  • Immunology
  • Hematology

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    Soprana, E., Vigo, E., Verani, A., Blom, J., Siccardi, A. G., Vercelli, D., & Viale, G. (1994). Antiidiotypic antibodies mimic molecular and functional properties of human IL-1β in vitro and in vivo. Lymphokine and Cytokine Research, 13(5), 325-330.