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  • Review Article
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Interactions between bacterial pathogens and mitochondrial cell death pathways

Nature Reviews Microbiology volume 8, pages 693–705 (2010)Cite this article

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Abstract

The modulation of host cell death pathways by bacteria has been recognized as a major pathogenicity mechanism. Among other strategies, bacterial pathogens can hijack the cell death machinery of host cells by influencing the signalling pathways that converge on the mitochondria. In particular, many bacterial proteins have evolved to interact in a highly specific manner with host mitochondria, thereby modulating the decision between cell life and death. In this Review, we explore the intimate interactions between bacterial pathogens and mitochondrial cell death pathways.

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Figure 1: Apoptotic cell death pathways.
Figure 2: Non-apoptotic cell death pathways.
Figure 3: Bacterial factors targeting mitochondria.
Figure 4: Cell death-modulating signalling pathways converging at the mitochondria.

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Acknowledgements

We thank L. Galluzzi for helpful advice during the preparation of the manuscript and L. Ogilvie for critically reading the manuscript.

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Authors and Affiliations

  1. Lehrstuhl für Mikrobiologie, Biozentrum der Universität Würzburg, Am Hubland, Würzburg, 97074, Germany

    Thomas Rudel & Vera Kozjak-Pavlovic

  2. INSERM U848, Institut Gustav Roussy, Faculté Sud-Université Paris 11, Villejuif, F-94804, France

    Oliver Kepp

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  1. Thomas Rudel
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  2. Oliver Kepp
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Correspondence to Thomas Rudel.

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FURTHER INFORMATION

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The caspase substrate database homepage

Glossary

Calreticulin

Ca2+-binding endoplasmic reticulum chaperone that under cell stress conditions can translocate to the cell surface and serve as an 'eat me' signal for dendritic cells.

Calpain

One of a group of Ca2+-activated cytoplasmic proteases that are found in many tissues and that hydrolyse various endogenous proteins.

Granzyme

A secreted serine protease that enters target cells through perforin pores, then cleaves and activates intracellular caspases, leading to apoptosis.

Perforin

A component of cytolytic granules that participates in the permeabilization of plasma membranes, allowing granzymes and other cytotoxic components to enter target cells.

T3SS

A bacterial secretion system that consists of a needle-like apparatus that transports proteins from the bacterial cytoplasm across the bacterial cell envelope directly into the eukaryotic cell cytoplasm.

T4SS

A multiprotein complex that mediates the translocation of macromolecules (proteins, DNA or DNA–protein) across the bacterial cell envelope into the extracellular medium or directly into recipient cells.

T5SS

Include both two-partner secretion systems and autotransporters. Two-partner secretion systems comprise two distinct proteins: a transporter protein and a secreted effector protein. Autotransporters are multidomain proteins that are secreted as precursors across the inner membrane by the Sec machinery. The translocator domain of the protein then inserts into the outer membrane and facilitates surface localization of the passenger domain.

TOM complex

A protein complex that recognizes nucleus-encoded mitochondrial pre-proteins and mediates their translocation across the membrane.

SAM complex

A protein complex that facilitates the integration of imported proteins into the outer mitochondrial membrane.

TIM complex

A protein complex in the inner membrane and intermembrane space of mitochondria that mediates transport of pre-proteins into and across the membrane.

Type IV pilus

An elongated, flexible appendage that extends from the surface of Gram-negative bacterial cells and is used for adhesion and twitching motility.

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Rudel, T., Kepp, O. & Kozjak-Pavlovic, V. Interactions between bacterial pathogens and mitochondrial cell death pathways. Nat Rev Microbiol 8, 693–705 (2010). https://doi.org/10.1038/nrmicro2421

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