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The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1

  1. Author:
    Hersh, D.
    Monack, D. M.
    Smith, M. R.
    Ghori, N.
    Falkow, S.
    Zychlinsky, A.

  2. Author Address

    Zychlinsky A NYU, Sch Med, Dept Microbiol, Skirball Inst 540 1st Ave New York, NY 10016 USA NYU, Sch Med, Dept Microbiol, Skirball Inst New York, NY 10016 USA NYU, Sch Med, Kaplan Canc Ctr New York, NY 10016 USA Stanford Univ, Sch Med, Dept Immunol & Microbiol Stanford, CA 94305 USA NCI, Intramural Res Support Program, Sci Applicat Int Corp, Frederick Canc Res & Dev Ctr Frederick, MD 21702 USA
    1. Year: 1999
  2. Journal: Proceedings of the National Academy of Sciences of the United States of America
    1. 96
    2. 5
    3. Pages: 2396-2401
  4. Type of Article: Article
  1. Abstract:

    Recently, Salmonella spp. were shown to induce apoptosis in infected macrophages. The mechanism responsible for this process is unknown. In this report, we establish that the Inv-Spa type III secretion apparatus target invasin SipB is necessary and sufficient for the induction of apoptosis. Purified SipB microinjected into macrophages led to cell death. Binding studies show that SipB associates with the proapoptotic protease caspase-1. This interaction results in the activation of caspase-1, as seen in its proteolytic maturation and the processing of its substrate interleukin-1 beta. Caspase-1 activity is essential for the cytotoxicity. Functional inhibition of caspase-1 activity by acetyl-Tyr-Val-Ala-Asp-chloromethyl ketone blocks macrophage cytotoxicity, and macrophages lacking caspase-1 are not susceptible to Salmonella-induced apoptosis. Taken together, the data demonstrate that SipB functions as an analog of the Shigella invasin IpaB. [References: 36]

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