The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Guanylate-binding proteins convert cytosolic bacteria into caspase-4 signaling platforms
Open accessAbstract
Bacterial lipopolysaccharide triggers human caspase-4 (murine caspase-11) to cleave gasdermin-D and induce pyroptotic cell death. How lipopolysaccharide sequestered in the membranes of cytosol-invading bacteria activates caspases remains unknown. Here we show that in interferon-γ-stimulated cells guanylate-binding proteins (GBPs) assemble on the surface of Gram-negative bacteria into polyvalent signaling platforms required for activation of caspase-4. Caspase-4 activation is hierarchically controlled by GBPs; GBP1 initiates platform assembly, GBP2 and GBP4 control caspase-4 recruitment, and GBP3 governs caspase-4 activation. In response to cytosol-invading bacteria, activation of caspase-4 through the GBP platform is essential to induce gasdermin-D-dependent pyroptosis and processing of interleukin-18, thereby destroying the replicative niche for intracellular bacteria and alerting neighboring cells, respectively. Caspase-11 and GBPs epistatically protect mice against lethal bacterial challenge. Multiple antagonists of the pathway encoded by Shigella flexneri, a cytosol-adapted bacterium, provide compelling evolutionary evidence for the importance of the GBP–caspase-4 pathway in antibacterial defense. How lipopolysaccharide embedded in bacterial membranes is sensed by intracellular defense mechanisms has been puzzling. Randow and colleagues show that guanylate-binding proteins assemble on the surface of Gram-negative bacteria to initiate downstream pyroptosis.
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Cites
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Cited by
A 360° view of the inflammasome: Mechanisms of activation, cell death, and diseases
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Ubiquitylation of lipopolysaccharide by RNF213 during bacterial infection
Otten, E. G., Werner, E., Crespillo-Casado, A., Boyle, K. B., Dharamdasani, V., Pathe, C., Santhanam, B., & Randow, F. (2021) · Nature · doi:10.1038/s41586-021-03566-4 · Cited by 394
Self-citationA Journey from Structure to Function of Bacterial Lipopolysaccharides
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Metadata
- Authors
- Wandel, M. P., Kim, B.-H., Park, E.-S., Boyle, K. B., Nayak, K., Lagrange, B., Herod, A., Henry, T., Zilbauer, M., Rohde, J., MacMicking, J. D., & Randow, F.
- Venue
- Nature Immunology
- Published
- 2020-06-15
- Volume
- 21
- Issue
- 8
- Pages
- 880-891
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- OpenAlex
- W3034751517
- Cited by
- 284
- References
- 49
- FWCI
- 11.69
- Type
- journal article
- Language
- en
- Open access
- green
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- Wandel, M. P., Kim, B.-H., Park, E.-S., Boyle, K. B., Nayak, K., Lagrange, B., Herod, A., Henry, T., Zilbauer, M., Rohde, J., MacMicking, J. D., & Randow, F. (2020). Guanylate-binding proteins convert cytosolic bacteria into caspase-4 signaling platforms. Nature Immunology. https://doi.org/10.1038/s41590-020-0697-2
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