The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida
Open accessAbstract
The AIM2 inflammasome detects double-stranded DNA in the cytosol and induces caspase-1-dependent pyroptosis as well as release of the inflammatory cytokines interleukin 1β (IL-1β) and IL-18. AIM2 is critical for host defense against DNA viruses and bacteria that replicate in the cytosol, such as Francisella tularensis subspecies novicida (F. novicida). The activation of AIM2 by F. novicida requires bacteriolysis, yet whether this process is accidental or is a host-driven immunological mechanism has remained unclear. By screening nearly 500 interferon-stimulated genes (ISGs) through the use of small interfering RNA (siRNA), we identified guanylate-binding proteins GBP2 and GBP5 as key activators of AIM2 during infection with F. novicida. We confirmed their prominent role in vitro and in a mouse model of tularemia. Mechanistically, these two GBPs targeted cytosolic F. novicida and promoted bacteriolysis. Thus, in addition to their role in host defense against vacuolar pathogens, GBPs also facilitate the presentation of ligands by directly attacking cytosolic bacteria.
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Cites
STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity
Ishikawa, H., Ma, Z., & Barber, G. N. (2009) · Nature · doi:10.1038/nature08476 · Cited by 2,759
AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
Hornung, V., Ablasser, A., Charrel-Dennis, M., Bauernfeind, F., Horvath, G., Caffrey, D. R., Latz, E., & Fitzgerald, K. A. (2009) · Nature · doi:10.1038/nature07725 · Cited by 2,627
AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
Fernandes-Alnemri, T., Yu, J.-W., Datta, P., Wu, J., & Alnemri, E. S. (2009) · Nature · doi:10.1038/nature07710 · Cited by 1,831
The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
Rathinam, V. A. K., Jiang, Z., Waggoner, S. N., Sharma, S., Cole, L. E., Waggoner, L., Vanaja, S. K., Monks, B. G., Ganesan, S., Latz, E., et al. (2010) · Nature Immunology · doi:10.1038/ni.1864 · Cited by 1,331
The AIM2 inflammasome is critical for innate immunity to Francisella tularensis
Fernandes-Alnemri, T., Yu, J.-W., Juliana, C., Solorzano, L., Kang, S., Wu, J., Datta, P., McCormick, M., Huang, L., McDermott, E., et al. (2010) · Nature Immunology · doi:10.1038/ni.1859 · Cited by 732
Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1
Broz, P., Ruby, T., Belhocine, K., Bouley, D. M., Kayagaki, N., Dixit, V. M., & Monack, D. M. (2012) · Nature · doi:10.1038/nature11419 · Cited by 535
A Family of IFN-γ–Inducible 65-kD GTPases Protects Against Bacterial Infection
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Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases
Meunier, E., Dick, M. S., Dreier, R. F., Schürmann, N., Broz, D. K., Warming, S., Roose-Girma, M., Bumann, D., Kayagaki, N., Takeda, K., et al. (2014) · Nature · doi:10.1038/nature13157 · Cited by 485
Self-citationGuanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS
Pilla, D. M., Hagar, J. A., Haldar, A. K., Mason, A. K., Degrandi, D., Pfeffer, K., Ernst, R. K., Yamamoto, M., Miao, E. A., & Coers, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321700111 · Cited by 357
Self-citationMycobacterium tuberculosis and the host cell inflammasome: a complex relationship
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Self-citationGaidt, M. M., Ebert, T. S., Chauhan, D., Ramshorn, K., Pinci, F., Zuber, S., O’Duill, F., Schmid-Burgk, J. L., Hoss, F., Buhmann, R., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.039 · Cited by 638
Genome-wide expression for diagnosis of pulmonary tuberculosis: a multicohort analysis
Sweeney, T. E., Braviak, L., Tato, C. M., & Khatri, P. (2016) · The Lancet Respiratory Medicine · doi:10.1016/s2213-2600(16)00048-5 · Cited by 445
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Metadata
- Authors
- Meunier, E., Wallet, P., Dreier, R. F., Costanzo, S., Anton, L., Rühl, S., Dussurgey, S., Dick, M. S., Kistner, A., Rigard, M., Degrandi, D., Pfeffer, K., Yamamoto, M., Henry, T., & Broz, P.
- Venue
- Nature Immunology
- Published
- 2015-03-16
- Volume
- 16
- Issue
- 5
- Pages
- 476-484
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- OpenAlex
- W1973288627
- Cited by
- 362
- References
- 10
- FWCI
- 17.88
- Type
- journal article
- Language
- en
- Open access
- green
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- Meunier, E., Wallet, P., Dreier, R. F., Costanzo, S., Anton, L., Rühl, S., Dussurgey, S., Dick, M. S., Kistner, A., Rigard, M., Degrandi, D., Pfeffer, K., Yamamoto, M., Henry, T., & Broz, P. (2015). Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida. Nature Immunology. https://doi.org/10.1038/ni.3119
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