Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12

Birgit Oppmann, Robin Lesley, Bianca Blom, Jackie C. Timans, Yuming Xu, Brisdell Hunte, Felix Vega, Nancy Yu, Jing Wang, Komal Singh, Francesca Zonin, Elena Vaisberg, Tatyana Churakova, Man ru Liu, Daniel Gorman, Janet Wagner, Sandra Zurawski, Yong Jun Liu, John S. Abrams, Kevin W. MooreDonna Rennick, Rene De Waal-Malefyt, Charles Hannum, J. Fernando Bazan, Robert A. Kastelein

Research output: Contribution to journalArticlepeer-review

2163 Scopus citations

Abstract

A novel sequence discovered in a computational screen appears distantly related to the p35 subunit of IL-12. This factor, which we term p19, shows no biological activity by itself; instead, it combines with the p40 subunit of IL-12 to form a novel, biologically active, composite cytokine, which we term IL-23. Activated dendritic cells secrete detectable levels of this complex. IL-23 binds to IL-12Rβ1 but fails to engage IL-12Rβ2; nonetheless, IL-23 activates Stat4 in PHA blast T cells. IL-23 induces strong proliferation of mouse memory (CD4+CD45Rb(low)) T cells, a unique activity of IL-23 as IL-12 has no effect on this cell population. Similar to IL-12, human IL-23 stimulates IFN-γ production and proliferation in PHA blast T cells, as well as in CD45RO (memory) T cells.

Original languageEnglish (US)
Pages (from-to)715-725
Number of pages11
JournalImmunity
Volume13
Issue number5
DOIs
StatePublished - Nov 2000
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases

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