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J Biol Chem, Vol. 273, Issue 49, 32895-32900, December 4, 1998

Shigella-induced Apoptosis Is Dependent on Caspase-1 Which Binds to IpaB

Hubert Hilbi, Jeremy E. Moss, David Hersh, Yajing Chen, Josette Arondel§, Subhashis Banerjee, Richard A. Flavellparallel , Junying YuanDagger Dagger , Philippe J. Sansonetti§, and Arturo Zychlinsky

From the Skirball Institute, Department of Microbiology and Kaplan Cancer Center, New York University School of Medicine, New York, New York 10016, the § Unité de Pathogénie Microbienne Moléculaire, INSERM U389, Institut Pasteur, 28 Rue du Docteur Roux, 75724 Paris Cedex 15, France,  BASF Bioresearch Corporation, Worcester, Massachusetts 01605-4314, the parallel  Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510, and the Dagger Dagger  Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115

We report here that the Shigella invasion plasmid antigen (Ipa)B, which is sufficient to induce apoptosis in macrophages, binds to caspase (Casp)-1, but not to Casp-2 or Casp-3. Casp-1 is activated and its specific substrate interleukin-1beta is cleaved shortly after Shigella infection. Macrophages isolated from Casp-1 knock-out mice are not susceptible to Shigella-induced apoptosis, although they respond normally to other apoptotic stimuli. Shigella kills macrophages from casp-3, casp-11, and p53 knock-out mice as well as macrophages overexpressing Bcl-2. We propose that Shigella induces apoptosis by directly activating Casp-1 through IpaB, bypassing signal transduction events and caspases upstream of Casp-1. Taken together these data indicate that Shigella-induced apoptosis is distinct from other forms of apoptosis and seems uniquely dependent on Casp-1.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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