Trends in Microbiology
Volume 9, Issue 2, 1 February 2001, Pages 64-67
Journal home page for Trends in Microbiology

Opinion
Salmonella-induced cell death: apoptosis, necrosis or programmed cell death?

https://doi.org/10.1016/S0966-842X(00)01937-5Get rights and content

Abstract

Over the past several years, it has become apparent that enteropathogens activate cell death programs. For Salmonella and Shigella species, the induction of cell death is required for pathogenesis, and the mechanisms by which these bacteria induce cell death is an area of intense investigation. Although initial studies suggested that Salmonella induce cell death through an apoptotic pathway, recent studies demonstrate that cell death occurs through a unique caspase 1-dependent mechanism.

Section snippets

Apoptosis: multiple pathways leading to the activation of caspases

Studies on developmental cell death in the nematode Caenorhabditis elegans indicate that a cysteine protease termed Ced-3 is required for PCD 6. In mammals, there are 14 known Ced-3-like proteases that comprise a family of proteins referred to as caspases (cysteine aspartases) 7. Based on structural features and substrate specificity, the mammalian caspases fall into three subclasses.

The first class is the downstream or effector caspases. These caspases are most similar to Ced-3, as they cleave

Salmonella-induced cell death

Salmonella typhi is the etiologic agent of typhoid fever in humans whereas S. typhimurium is known to cause a typhoid-like disease in mice. The organisms are taken up by ingestion of contaminated food, and enter the digestive tract. Once they reach the lower gastrointestinal tract, they cross through the M cells that overlay the Peyer's patches and gain access to the lymphoid follicles and lamina propria. There, the Salmonella enter macrophages and reside in vesicles. Inside these vesicles, the

Acknowledgments

We thank Mike Starnbach, Adrianus van der Velden and Enrique Cepero for their comments.

References (26)

  • N.A Thornberry et al.

    Caspases: enemies within

    Science

    (1998)
  • G.S Salvesen et al.

    Caspase activation: the induced-proximity model

    Proc. Natl. Acad. Sci. USA

    (1999)
  • F.C Kischkel

    Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC)

    EMBO J.

    (1995)
  • Cited by (129)

    • The emerging role of pyroptosis in neuropathic pain

      2023, International Immunopharmacology
    • JQ1 attenuates neuroinflammation by inhibiting the inflammasome-dependent canonical pyroptosis pathway in SAE

      2022, Brain Research Bulletin
      Citation Excerpt :

      This type of cell death was recently suggested to be dependent on nod-like receptor family protein 1 (NLRP1) or 3 (NLRP3) or absent in melanoma 2 (AIM2) inflammasomes, which can further trigger pyroptosis signalling pathways (Dempsey et al., 2017; Fan et al., 2018). Pyroptosis is executed by a series of pore-forming proteins called the gasdermin superfamily (GSDMs) (Boise and Collins, 2001), including gasdermin A (GSDMA), gasdermin B (GSDMB), gasdermin C (GSDMC), gasdermin D (GSDMD), gasdermin E (GSDME) and pejvakin (PJVK). Except for PJVK (Rogers et al., 2019), all members of the GSDM superfamily contain a conserved two-domain structure: the N-terminal and C-terminal domains.

    View all citing articles on Scopus
    View full text