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The Journal of Immunology, 2000, 164: 4672-4677.
Copyright © 2000 by The American Association of Immunologists

IL-6 Receptor Independent Stimulation of Human gp130 by Viral IL-61

Jürgen Müllberg2,*,3, Till Geib2,*, Thomas Jostock2,*, Susanne H. Hoischen*, Petra Vollmer*, Nicole Voltz*, David Heinz*, Peter R. Galle*, Mariam Klouche{dagger} and Stefan Rose-John4,*

* I. Medizinische Klinik, Abteilung Pathophysiologie, and {dagger} Institut für Medizinische Microbiologie und Hygiene, Johannes Gutenberg-Universität Mainz, Mainz, Germany

The genome of human herpes virus 8, which is associated with Kaposi’s sarcoma, encodes proteins with similarities to cytokines and chemokines including a homologue of IL-6. Although the function of these viral proteins is unclear, they might have the potential to modulate the immune system. For viral IL-6 (vIL-6), it has been demonstrated that it stimulates IL-6-dependent cells, indicating that the IL-6R system is used. IL-6 binds to IL-6R, and the IL-6/IL-6R complex associates with gp130 which dimerizes and initiates intracellular signaling. Cells that only express gp130 but no IL-6R cannot be stimulated by IL-6 unless a soluble form of the IL-6R is present. This type of signaling has been shown for hematopoietic progenitor cells, endothelial cells, and smooth muscle cells. In this paper we show that purified recombinant vIL-6 binds to gp130 and stimulates primary human smooth muscle cells. IL-6R fails to bind vIL-6 and is not involved in its signaling. A Fc fusion protein of gp130 turned out to be a potent inhibitor of vIL-6. Our data demonstrate that vIL-6 is the first cytokine which directly binds and activates gp130. This property points to a possible role of this viral cytokine in the pathophysiology of human herpes virus 8.




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