Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS
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Significance: A major component of the cell envelope of Gram-negative bacteria is LPS, also known as endotoxin. LPS produced during bacterial infections triggers inflammation, which can lead to septic shock and death. Our immune system can recognize LPS both outside and inside of cells. The recognition of extracellular and vacuolar LPS by LPS binding proteins is well described, but little is known about the recognition of cytoplasmic LPS. Here, we show that cytoplasmic LPS derived from the intracellular bacterial pathogen Legionella activated a proinflammatory immune response. We further identified host guanylate binding proteins as critical mediators of immunity triggered by cytoplasmic LPS. These findings are likely to advance our understanding of how cells can sense intracellular LPS.
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Type I IFN and IFNG contribute to pyroptosis by promoting expression of guanylate-binding proteins and IRGB10, which increase cytosolic LPS levels by mediating lysis of vacuoles containing Gram-negative bacteria.
“(3) the expression of guanylate-binding proteins and an IFN-inducible GTPase commonly known as IRGB10 (official name Gm12250), which increase cytosolic LPS levels by mediating the lysis of vacuoles containing Gram-negative bacteria [646–648].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [647]
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A SIMPLE METHOD FOR THE ISOLATION AND PURIFICATION OF TOTAL LIPIDES FROM ANIMAL TISSUES
Folch, J., Lees, M., & Stanley, G. H. S. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64849-5 · Cited by 65,189 · see citing works
Non-canonical inflammasome activation targets caspase-11
Kayagaki, N., Warming, S., Lamkanfi, M., Walle, L. V., Louie, S., Dong, J., Newton, K., Qu, Y., Liu, J., Heldens, S., et al. (2011) · Nature · doi:10.1038/nature10558 · Cited by 2,530 · see citing works
Noncanonical Inflammasome Activation by Intracellular LPS Independent of TLR4
Kayagaki, N., Wong, M. T., Stowe, I. B., Ramani, S. R., Gonzalez, L. C., Akashi‐Takamura, S., Miyake, K., Zhang, J., Lee, W. P., Muszyński, A., et al. (2013) · Science · doi:10.1126/science.1240248 · Cited by 1,544 · see citing works
Cytoplasmic LPS Activates Caspase-11: Implications in TLR4-Independent Endotoxic Shock
Hagar, J. A., Powell, D. A., Aachoui, Y., Ernst, R. K., & Miao, E. A. (2013) · Science · doi:10.1126/science.1240988 · Cited by 1,265 · see citing works
Self-citationHirschfeld, M. J., Ma, Y., Weis, J. H., Vogel, S. N., & Weis, J. J. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.2.618 · Cited by 1,155 · see citing works
LPS, TLR4 and infectious disease diversity
Miller, S., Ernst, R. K., & Bader, M. W. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1068 · Cited by 1,059 · see citing works
Self-citationGalectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
Thurston, T. L. M., Wandel, M. P., von Muhlinen, N., Foeglein, Á., & Randow, F. (2012) · Nature · doi:10.1038/nature10744 · Cited by 1,034 · see citing works
Sensing and reacting to microbes through the inflammasomes
Franchi, L., Muñoz-Planillo, R., & Núñez, G. (2012) · Nature Immunology · doi:10.1038/ni.2231 · Cited by 1,013 · see citing works
TRIF Licenses Caspase-11-Dependent NLRP3 Inflammasome Activation by Gram-Negative Bacteria
Rathinam, V. A. K., Vanaja, S. K., Waggoner, L., Sokolovska, A., Becker, C., Stuart, L. M., Leong, J. M., & Fitzgerald, K. A. (2012) · Cell · doi:10.1016/j.cell.2012.07.007 · Cited by 729 · see citing works
Berger, K. H., & Isberg, R. R. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01092.x · Cited by 646 · see citing works
Charcoal-yeast extract agar: primary isolation medium for Legionella pneumophila
FEELEY, J. C., Gibson, R. J., GORMAN, G. W., Langford, N. C., Rasheed, J. K., Mackel, D. C., & Baine, W. B. (1979) · Journal of Clinical Microbiology · doi:10.1128/jcm.10.4.437-441.1979 · Cited by 643 · see citing works
Salmonella maintains the integrity of its intracellular vacuole through the action of SifA
Beuzón, C. R., Méresse, S., Unsworth, K. E., Ruiz‐Albert, J., Garvis, S., Waterman, S. R., Ryder, T. A., Boucrot, E., & Holden, D. W. (2000) · The EMBO Journal · doi:10.1093/emboj/19.13.3235 · Cited by 595 · see citing works
Interferon-inducible effector mechanisms in cell-autonomous immunity
MacMicking, J. D. (2012) · Nature reviews. Immunology · doi:10.1038/nri3210 · Cited by 564 · see citing works
Caspase-11 Protects Against Bacteria That Escape the Vacuole
Aachoui, Y., Leaf, I. A., Hagar, J. A., Fontana, M. F., Campos, C. G., Zak, D. E., Tan, M. H., Cotter, P. A., Vance, R. E., Aderem, A. A., et al. (2013) · Science · doi:10.1126/science.1230751 · Cited by 544 · see citing works
Self-citationFlagellin-Deficient Legionella Mutants Evade Caspase-1- and Naip5-Mediated Macrophage Immunity
Ren, T., Zamboni, D. S., Roy, C. R., Dietrich, W. F., & Vance, R. E. (2006) · PLoS Pathogens · doi:10.1371/journal.ppat.0020018 · Cited by 536 · see citing works
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 · see citing works
Zamboni, D. S., Kobayashi, K. S., Kohlsdorf, T., Ogura, Y., Long, E. M., Vance, R. E., Kuida, K., Mariathasan, S., Dixit, V. M., Flavell, R. A., et al. (2006) · Nature Immunology · doi:10.1038/ni1305 · Cited by 515 · see citing works
GBP5 Promotes NLRP3 Inflammasome Assembly and Immunity in Mammals
Shenoy, A. R., Wellington, D. A., Kumar, P., Kassa, H. T., Booth, C. J., Cresswell, P., & MacMicking, J. D. (2012) · Science · doi:10.1126/science.1217141 · Cited by 512 · see citing works
Cytosolic recognition of flagellin by mouse macrophages restricts Legionella pneumophila infection
Molofsky, A. B., Byrne, B. G., Whitfield, N. N., Madigan, C. A., Fuse, E. T., Tateda, K., & Swanson, M. S. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20051659 · Cited by 490 · see citing works
Galectin-3, a marker for vacuole lysis by invasive pathogens
Paz, I., Sachse, M., Dupont, N., Mounier, J., Cederfur, C., Enninga, J., Leffler, H., Poirier, F., Prévost, M., Lafont, F., et al. (2009) · Cellular Microbiology · doi:10.1111/j.1462-5822.2009.01415.x · Cited by 384 · see citing works
Expression of Legionella pneumophila Virulence Traits in Response to Growth Conditions
Byrne, B. G., & Swanson, M. S. (1998) · Infection and Immunity · doi:10.1128/iai.66.7.3029-3034.1998 · Cited by 364 · see citing works
Disruption of Toxoplasma gondii Parasitophorous Vacuoles by the Mouse p47-Resistance GTPases
Martens, S., Parvanova, I., Zerrahn, J., Griffiths, G. W., Schell, G., Reichmann, G., & Howard, J. C. (2005) · PLoS Pathogens · doi:10.1371/journal.ppat.0010024 · Cited by 356 · see citing works
Ling, Y. M., Shaw, M. H., Ayala, C. A., Coppens, I., Taylor, G. A., Ferguson, D. J. P., & Yap, G. S. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20061318 · Cited by 350 · see citing works
Yamamoto, M., Okuyama, M., Su, J., Kimura, T., Kamiyama, N., Saiga, H., Ohshima, J., Sasai, M., Kayama, H., Okamoto, T., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.06.009 · Cited by 330 · see citing works
Self-citationStructure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins
Prakash, B., Praefcke, G. J. K., Renault, L., Wittinghofer, A., & Herrmann, C. (2000) · Nature · doi:10.1038/35000617 · Cited by 325 · see citing works
Listeriolysin O: the Swiss army knife of Listeria
Hamon, M. A., Ribet, D., Stavru, F., & Cossart, P. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2012.04.006 · Cited by 295 · see citing works
Caspase-11 stimulates rapid flagellin-independent pyroptosis in response to Legionella pneumophila
Case, C. L., Kohler, L. J., Lima, J. B., Strowig, T., de Zoete, M. R., Flavell, R. A., Zamboni, D. S., & Roy, C. R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1211521110 · Cited by 275 · see citing works
Molecular mechanisms of inflammasome activation during microbial infections
Brož, P., & Monack, D. M. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01041.x · Cited by 257 · see citing works
The protein SdhA maintains the integrity of the Legionella -containing vacuole
Creasey, E. A., & Isberg, R. R. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121286109 · Cited by 198 · see citing works
Murine Guanylate Binding Protein 2 (mGBP2) controls Toxoplasma gondii replication
Degrandi, D., Kravets, E., Konermann, C., Beuter-Gunia, C., Klümpers, V., Lahme, S., Rasch, E., Mausberg, A. K., Beer‐Hammer, S., & Pfeffer, K. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205635110 · Cited by 196 · see citing works
Self-citationCaspase-11 Activation in Response to Bacterial Secretion Systems that Access the Host Cytosol
Casson, C. N., Copenhaver, A. M., Zwack, E. E., Nguyen, H. T., Strowig, T., Javdan, B., Bradley, W. P., Fung, T. C., Flavell, R. A., Brodsky, I. E., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003400 · Cited by 178 · see citing works
Schauvliege, R., Vanrobaeys, J., Schotte, P., & Beyaert, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207852200 · Cited by 162 · see citing works
Girard, R., Pédron, T., Uematsu, S., Balloy, V., Chignard, M., Akira, S., & Chaby, R. (2002) · Journal of Cell Science · doi:10.1242/jcs.00212 · Cited by 150 · see citing works
Coers, J., Vance, R. E., Fontana, M. F., & Dietrich, W. F. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.00963.x · Cited by 146 · see citing works
Self-citationLegionella pneumophila pathogenesis and immunity
Friedman, H. P., Yamamoto, Y., & Klein, T. (2002) · Seminars in Pediatric Infectious Diseases · doi:10.1053/spid.2002.127206 · Cited by 112 · see citing works
Dissection of a type I interferon pathway in controlling bacterial intracellular infection in mice
Lippmann, J., Müller, H. C., Naujoks, J., Tabeling, C., Shin, S., Witzenrath, M., Hellwig, K., Kirschning, C. J., Taylor, G. A., Barchet, W., et al. (2011) · Cellular Microbiology · doi:10.1111/j.1462-5822.2011.01646.x · Cited by 87 · see citing works
Killing of Legionella pneumophila by nitric oxide in γ-interferon-activated macrophages
Summersgill, J. T., Powell, L. A., Buster, B. L., Miller, R. D., & Ramírez, J. A. (1992) · Journal of Leukocyte Biology · doi:10.1002/jlb.52.6.625 · Cited by 77 · see citing works
Miao, E. A., Freeman, J. A., & Miller, S. I. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.5.1493-1497.2002 · Cited by 63 · see citing works
Self-citationPrincipato, M. A., Cleveland, J. L., Rapp, U. R., Holmes, K. L., Pierce, J. H., Morse, H. C., & Klinken, S. P. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.7.3562 · Cited by 61 · see citing works
Lettinga, K. D., Florquin, S., Speelman, P., Ketel, R. J. V., van der Poll, T., & Verbon, A. (2002) · The Journal of Infectious Diseases · doi:10.1086/341780 · Cited by 57 · see citing works
Lück, C., Fry, N. K., Helbig, J. H., Jarraud, S., & Harrison, T. G. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-161-5_6 · Cited by 51 · see citing works
Coers, J., Gondek, D. C., Olive, A. J., Rohlfing, A. E., Taylor, G. A., & Starnbach, M. N. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1001346 · Cited by 45 · see citing works
Self-citationCharacterization of Legionella Lipopolysaccharide
Lück, C., & Helbig, J. H. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-161-5_24 · Cited by 16 · see citing works
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Sorted by citations
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works
Inflammasomes: mechanism of assembly, regulation and signalling
Broz, P., & Dixit, V. M. (2016) · Nature Reviews Immunology · doi:10.1038/nri.2016.58 · Cited by 3,500 · see citing works
Inflammatory caspases are innate immune receptors for intracellular LPS
Shi, J., Zhao, Y., Wang, Y., Gao, W., Ding, J., Li, P., Hu, L., & Shao, F. (2014) · Nature · doi:10.1038/nature13683 · Cited by 2,285 · see citing works
Man, S. M., Karki, R., & Kanneganti, T. (2017) · Immunological Reviews · doi:10.1111/imr.12534 · Cited by 1,659 · see citing works
Gosselin, D., Link, V. M., Romanoski, C. E., Fonseca, G. J., Eichenfield, D. Z., Spann, N. J., Stender, J. D., Chun, H. B., Garner, H., Geissmann, F., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.023 · Cited by 1,307 · see citing works
Caspases in Cell Death, Inflammation, and Disease
Opdenbosch, N. V., & Lamkanfi, M. (2019) · Immunity · doi:10.1016/j.immuni.2019.05.020 · Cited by 1,230 · see citing works
Inflammasome Complexes: Emerging Mechanisms and Effector Functions
Rathinam, V. A. K., & Fitzgerald, K. A. (2016) · Cell · doi:10.1016/j.cell.2016.03.046 · Cited by 1,109 · see citing works
Regulation of inflammasome activation
Man, S. M., & Kanneganti, T. (2015) · Immunological Reviews · doi:10.1111/imr.12296 · Cited by 1,071 · see citing works
Pyroptotic cell death defends against intracellular pathogens
Jorgensen, I., & Miao, E. A. (2015) · Immunological Reviews · doi:10.1111/imr.12287 · Cited by 1,021 · see citing works
Self-citationConverging roles of caspases in inflammasome activation, cell death and innate immunity
Man, S. M., & Kanneganti, T. (2015) · Nature reviews. Immunology · doi:10.1038/nri.2015.7 · Cited by 701 · see citing works
Innate immunity to intracellular LPS
Rathinam, V. A. K., Zhao, Y., & Shao, F. (2019) · Nature Immunology · doi:10.1038/s41590-019-0368-3 · Cited by 606 · see citing works
Yang, D., He, Y., Muñoz-Planillo, R., Liu, Q., & Núñez, G. (2015) · Immunity · doi:10.1016/j.immuni.2015.10.009 · Cited by 602 · see citing works
Regulated cell death and inflammation: an auto-amplification loop causes organ failure
Linkermann, A., Stockwell, B. R., Krautwald, S., & Anders, H.-J. (2014) · Nature Reviews Immunology · doi:10.1038/nri3743 · Cited by 522 · see citing works
Mechanisms of inflammasome activation: recent advances and novel insights
Vanaja, S. K., Rathinam, V. A. K., & Fitzgerald, K. A. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.12.009 · Cited by 499 · see citing works
Inflammasome activation and assembly at a glance
Malik, A., & Kanneganti, T. (2017) · Journal of Cell Science · doi:10.1242/jcs.207365 · Cited by 451 · see citing works
Recent Advances in Lipopolysaccharide Recognition Systems
Mazgaeen, L., & Gurung, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020379 · Cited by 382 · see citing works
Meunier, É., Wallet, P., Dreier, R. F., Costanzo, S., Anton, L., Rühl, S., Dussurgey, S., Dick, M. S., Kistner, A., Mélanie, R., et al. (2015) · Nature Immunology · doi:10.1038/ni.3119 · Cited by 353 · see citing works
Self-citationStructure and function: Lipid A modifications in commensals and pathogens
Steimle, A., Autenrieth, I. B., & Frick, J.-S. (2016) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2016.03.001 · Cited by 357 · see citing works
Interferon-induced guanylate-binding proteins: Guardians of host defense in health and disease
Tretina, K., Park, E., Mamińska, A., & MacMicking, J. D. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20182031 · Cited by 323 · see citing works
An overview of the non-canonical inflammasome
Downs, K. P., Nguyen, H., Dorfleutner, A., & Stehlik, C. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100924 · Cited by 328 · see citing works
The role of lipopolysaccharide-induced cell signalling in chronic inflammation
Page, M. J., Kell, D. B., & Pretorius, E. (2022) · Chronic Stress · doi:10.1177/24705470221076390 · Cited by 315 · see citing works
Roles of Caspases in Necrotic Cell Death
Yuan, J., Najafov, A., & Py, B. F. (2016) · Cell · doi:10.1016/j.cell.2016.11.047 · Cited by 290 · see citing works
Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria
Santos, J. C., Boucher, D., Kapinos, L. E., Demarco, B., Dilucca, M., Shkarina, K., Heilig, R., Chen, K. W., Lim, R. Y. H., & Brož, P. (2020) · Nature Communications · doi:10.1038/s41467-020-16889-z · Cited by 281 · see citing works
Guanylate-binding proteins convert cytosolic bacteria into caspase-4 signaling platforms
Wandel, M. P., Kim, B.-H., Park, E., Boyle, K. B., Nayak, K., Lagrange, B., Herod, A., Henry, T., Zilbauer, M., Rohde, J. R., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0697-2 · Cited by 282 · see citing works
The Role of Interferons in Inflammation and Inflammasome Activation
Kopitar‐Jerala, N. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00873 · Cited by 280 · see citing works
Casson, C. N., Yu, J. M., Reyes, V. M., Taschuk, F., Yadav, A., Copenhaver, A. M., Nguyen, H. T., Collman, R. G., & Shin, S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421699112 · Cited by 276 · see citing works
Non-canonical activation of inflammatory caspases by cytosolic LPS in innate immunity
Yang, J., Zhao, Y., & Shao, F. (2015) · Current Opinion in Immunology · doi:10.1016/j.coi.2015.01.007 · Cited by 269 · see citing works
Naujoks, J., Tabeling, C., Dill, B. D., Hoffmann, C., Brown, A. S., Kunze, M., Kempa, S., Peter, A., Mollenkopf, H.-J., Dorhoi, A., et al. (2016) · PLOS Pathogens · doi:10.1371/journal.ppat.1005408 · Cited by 261 · see citing works
Yi, Y. (2017) · Immunology · doi:10.1111/imm.12787 · Cited by 250 · see citing works
Santos, J. C., Dick, M. S., Lagrange, B., Degrandi, D., Pfeffer, K., Yamamoto, M., Meunier, É., Pelczar, P., Henry, T., & Brož, P. (2018) · The EMBO Journal · doi:10.15252/embj.201798089 · Cited by 238 · see citing works
Self-citationZamyatina, A., & Heine, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.585146 · Cited by 243 · see citing works
Inflammasomes and adaptive immune responses
Deets, K. A., & Vance, R. E. (2021) · Nature Immunology · doi:10.1038/s41590-021-00869-6 · Cited by 238 · see citing works
Human GBP1 is a microbe‐specific gatekeeper of macrophage apoptosis and pyroptosis
Fisch, D., Bando, H., Clough, B., Hornung, V., Yamamoto, M., Shenoy, A. R., & Frickel, E. (2019) · The EMBO Journal · doi:10.15252/embj.2018100926 · Cited by 222 · see citing works
Self-citationInterferon-Inducible GTPases in Host Resistance, Inflammation and Disease
Pilla-Moffett, D. M., Barber, M. F., Taylor, G. A., & Coers, J. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.04.032 · Cited by 216 · see citing works
Self-citationUbiquitination and degradation of GBPs by a Shigella effector to suppress host defence
Li, P., Jiang, W., Yu, Q., Liu, W., Zhou, P., Li, J., Xu, J., Xu, B., Wang, F., & Shao, F. (2017) · Nature · doi:10.1038/nature24467 · Cited by 206 · see citing works
Shigella evades pyroptosis by arginine ADP-riboxanation of caspase-11
Li, Z., Liu, W., Fu, J., Cheng, S., Xu, Y., Wang, Z., Liu, X., Shi, X., Liu, Y., Qi, X., et al. (2021) · Nature · doi:10.1038/s41586-021-04020-1 · Cited by 190 · see citing works
Lagrange, B., Benaoudia, S., Wallet, P., Magnotti, F., Provost, A., Michal, F., Martin, A., Lorenzo, F. D., Py, B. F., Molinaro, A., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02682-y · Cited by 194 · see citing works
Molecular mechanisms of inflammasome signaling
Mathur, A., Hayward, J. A., & Man, S. M. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.3mr0617-250r · Cited by 189 · see citing works
Mechanistic insights into gasdermin-mediated pyroptosis
Bai, Y., Pan, Y., & Liu, X. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00837-0 · Cited by 198 · see citing works
Direct binding of polymeric GBP1 to LPS disrupts bacterial cell envelope functions
Kutsch, M., Sistemich, L., Lesser, C. F., Goldberg, M. B., Herrmann, C., & Coers, J. (2020) · The EMBO Journal · doi:10.15252/embj.2020104926 · Cited by 169 · see citing works
Self-citationFunction and Regulation of Noncanonical Caspase-4/5/11 Inflammasome
Matikainen, S., Nyman, T. A., & Cypryk, W. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000373 · Cited by 175 · see citing works
Haldar, A. K., Foltz, C., Finethy, R., Piro, A. S., Feeley, E. M., Pilla-Moffett, D. M., Komatsu, M., Frickel, E., & Coers, J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1515966112 · Cited by 169 · see citing works
Self-citationCaspase-11 auto-proteolysis is crucial for noncanonical inflammasome activation
Lee, B. L., Stowe, I. B., Gupta, A., Kornfeld, O. S., Roose‐Girma, M., Anderson, K. R., Warming, S., Zhang, J., Lee, W. P., & Kayagaki, N. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20180589 · Cited by 167 · see citing works
Cytosolic Recognition of Microbes and Pathogens: Inflammasomes in Action
Hayward, J. A., Mathur, A., Ngo, C., & Man, S. M. (2018) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00015-18 · Cited by 163 · see citing works
Caspase crosstalk: integration of apoptotic and innate immune signalling pathways
Creagh, E. M. (2014) · Trends in Immunology · doi:10.1016/j.it.2014.10.004 · Cited by 160 · see citing works
Interferon-induced guanylate-binding proteins in inflammasome activation and host defense
Kim, B.-H., Chee, J., Bradfield, C. J., Park, E., Kumar, P., & MacMicking, J. D. (2016) · Nature Immunology · doi:10.1038/ni.3440 · Cited by 161 · see citing works
Inflammasome Activation by Bacterial Outer Membrane Vesicles Requires Guanylate Binding Proteins
Finethy, R., Luoma, S., Orench‐Rivera, N., Feeley, E. M., Haldar, A. K., Yamamoto, M., Kanneganti, T., Kuehn, M. J., & Coers, J. (2017) · mBio · doi:10.1128/mbio.01188-17 · Cited by 154 · see citing works
Self-citationFinethy, R., Jørgensen, I., Haldar, A. K., de Zoete, M. R., Strowig, T., Flavell, R. A., Yamamoto, M., Nagarajan, U. M., Miao, E. A., & Coers, J. (2015) · Infection and Immunity · doi:10.1128/iai.00856-15 · Cited by 147 · see citing works
Self-citationFeeley, E. M., Pilla-Moffett, D. M., Zwack, E. E., Piro, A. S., Finethy, R., Kolb, J. P., Martinez, J., Brodsky, I. E., & Coers, J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615771114 · Cited by 148 · see citing works
Self-citationNow you see me, now you don't: the interaction of Salmonella with innate immune receptors
Keestra, A. M., Tsolis, R. M., & Bäumler, A. J. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3428 · Cited by 142 · see citing works
Innate, adaptive, and cell-autonomous immunity against Toxoplasma gondii infection
Sasai, M., & Yamamoto, M. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0353-9 · Cited by 149 · see citing works
Self-citationRecent Insights on Inflammasomes, Gasdermin Pores, and PyroptosisPreprint
de Vasconcelos, N. M., & Lamkanfi, M. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a036392 · Cited by 139 · see citing works
Intracellular Lipopolysaccharide Sensing as a Potential Therapeutic Target for Sepsis
Pfalzgraff, A., & Weindl, G. (2019) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2019.01.001 · Cited by 139 · see citing works
Outer Membrane Lipid Secretion and the Innate Immune Response to Gram-Negative Bacteria
Giordano, N. P., Cian, M. B., & Dalebroux, Z. D. (2020) · Infection and Immunity · doi:10.1128/iai.00920-19 · Cited by 138 · see citing works
Guanylate binding proteins directly attack Toxoplasma gondii via supramolecular complexes
Kravets, E., Degrandi, D., Ma, Q., Peulen, T.-O., Klümpers, V., Felekyan, S., Kühnemuth, R., Weidtkamp‐Peters, S., Seidel, C. A. M., & Pfeffer, K. (2016) · eLife · doi:10.7554/elife.11479 · Cited by 134 · see citing works
Self-citationLipid Droplet, a Key Player in Host-Parasite Interactions
Vallochi, A. L., Teixeira, L., Oliveira, K. D. S., Maya‐Monteiro, C. M., & Bozza, P. T. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01022 · Cited by 133 · see citing works
Growth inhibition of cytosolic Salmonella by caspase-1 and caspase-11 precedes host cell death
Thurston, T. L. M., Matthews, S. A., Jennings, E. R., Alix, E., Shao, F., Shenoy, A. R., Birrell, M. A., & Holden, D. W. (2016) · Nature Communications · doi:10.1038/ncomms13292 · Cited by 137 · see citing works
Aachoui, Y., Kajiwara, Y., Leaf, I. A., Mao, D., Ting, J. P.-Y., Coers, J., Aderem, A., Buxbaum, J. D., & Miao, E. A. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.07.016 · Cited by 125 · see citing works
Self-citationBacterial recognition pathways that lead to inflammasome activation
Storek, K. M., & Monack, D. M. (2015) · Immunological Reviews · doi:10.1111/imr.12289 · Cited by 129 · see citing works
Piro, A. S., Hernandez, D., Luoma, S., Feeley, E. M., Finethy, R., Yirga, A., Frickel, E., Lesser, C. F., & Coers, J. (2017) · mBio · doi:10.1128/mbio.01979-17 · Cited by 125 · see citing works
Self-citationInterferon-inducible GTPases in cell autonomous and innate immunity
Meunier, É., & Brož, P. (2015) · Cellular Microbiology · doi:10.1111/cmi.12546 · Cited by 118 · see citing works
Effector-triggered immunity and pathogen sensing in metazoans
Fischer, N. L., Naseer, N., Shin, S., & Brodsky, I. E. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0623-2 · Cited by 118 · see citing works
Regulation of innate immune functions by guanylate-binding proteins
Praefcke, G. J. K. (2017) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2017.10.013 · Cited by 118 · see citing works
Guanylate-Binding Protein 1: An Emerging Target in Inflammation and Cancer
Honkala, A. T., Tailor, D., & Malhotra, S. V. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2019.03139 · Cited by 118 · see citing works
Salmonella enterica: living a double life in epithelial cells
Knodler, L. A. (2014) · Current Opinion in Microbiology · doi:10.1016/j.mib.2014.10.010 · Cited by 114 · see citing works
Innate Immunity to Intracellular Pathogens: Balancing Microbial Elimination and Inflammation
Mitchell, G., & Isberg, R. R. (2017) · Cell Host & Microbe · doi:10.1016/j.chom.2017.07.005 · Cited by 107 · see citing works
Stressing out the mitochondria: Mechanistic insights into NLRP3 inflammasome activation
Yabal, M., Calleja, D. J., Simpson, D. S., & Lawlor, K. E. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.mr0318-124r · Cited by 109 · see citing works
Man, S. M., Place, D. E., Kuriakose, T., & Kanneganti, T. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.4mr0516-223r · Cited by 108 · see citing works
Fisch, D., Clough, B., Domart, M., Encheva, V., Bando, H., Snijders, A. P., Collinson, L., Yamamoto, M., Shenoy, A. R., & Frickel, E. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108008 · Cited by 110 · see citing works
Self-citationInflammasome activation in acute lung injury
McVey, M. J., Steinberg, B. E., & Goldenberg, N. M. (2020) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00303.2020 · Cited by 108 · see citing works
Koltes, J. E., Fritz-Waters, E. R., Eisley, C. J., Choi, I., Bao, H., Kommadath, A., Serão, N. V. L., Boddicker, N. J., Abrams, S. M., Schroyen, M., et al. (2015) · BMC Genomics · doi:10.1186/s12864-015-1635-9 · Cited by 105 · see citing works
Regulating metabolic inflammation by nutritional modulation
Charles‐Messance, H., Mitchelson, K. A. J., Castro, E. D. M., Sheedy, F. J., & Roche, H. M. (2020) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2020.08.013 · Cited by 113 · see citing works
Increasing complexity of NLRP3 inflammasome regulation
Moretti, J., & Blander, J. M. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mr0520-104rr · Cited by 101 · see citing works
Lupfer, C. R., Anand, P., Liu, Z., Stokes, K. L., Vogel, P., Lamkanfi, M., & Kanneganti, T. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004410 · Cited by 97 · see citing works
Cerqueira, D. M., Gomes, M. T. R., Silva, A. L. N., Rungue, M., Assis, N. R. G., Guimarães, E. S., Morais, S. B., Brož, P., Zamboni, D. S., & Oliveira, S. C. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007519 · Cited by 95 · see citing works
Huang, X., Feng, Y., Xiong, G., Whyte, S. K., Duan, J., Yang, Y., Wang, K., Yang, S., Geng, Y., Ou, Y., et al. (2019) · Cell & Bioscience · doi:10.1186/s13578-019-0292-0 · Cited by 93 · see citing works
Crowley, S. M., Han, X., Allaire, J. M., Stahl, M., Rauch, I., Knodler, L. A., & Vallance, B. A. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008498 · Cited by 92 · see citing works
Dubey, S. R., Turnbull, C., Pandey, A., Zhao, A., Kurera, M., Al-Zidan, R. N., Shen, C. X., Gautam, M., Mahajan, S., Jadhav, P. S., et al. (2025) · Cellular and Molecular Immunology · doi:10.1038/s41423-025-01354-y · Cited by 97 · see citing works
Exposing Toxoplasma gondii hiding inside the vacuole: a role for GBPs, autophagy and host cell death
Saeij, J. P. J., & Frickel, E. (2017) · Current Opinion in Microbiology · doi:10.1016/j.mib.2017.10.021 · Cited by 89 · see citing works
Kim, B.-R., Kim, B.-J., Kook, Y., & Kim, B. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008294 · Cited by 89 · see citing works
A genome‐wide screen identifies IRF2 as a key regulator of caspase‐4 in human cells
Benaoudia, S., Martin, A., Gámez, M. P., Gay, G., Lagrange, B., Cornut, M., Krasnykov, K., Claude, J., Bourgeois, C. F., Hughes, S., et al. (2019) · EMBO Reports · doi:10.15252/embr.201948235 · Cited by 88 · see citing works
Role of pyroptosis in liver diseases
Mamun, A. A., Wu, Y., Jia, C., Munir, F., Sathy, K. J., Sarker, T., Monalisa, I., Zhou, K., & Xiao, J. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.106489 · Cited by 89 · see citing works
Human guanylate binding proteins: nanomachines orchestrating host defense
Kutsch, M., & Coers, J. (2020) · FEBS Journal · doi:10.1111/febs.15662 · Cited by 83 · see citing works
Self-citationLiu, B. C., Sarhan, J., Panda, A., Muendlein, H. I., Ilyukha, V., Coers, J., Yamamoto, M., Isberg, R. R., & Poltorak, A. N. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.012 · Cited by 80 · see citing works
Self-citationTyrkalska, S. D., Pérez‐Oliva, A. B., Rodríguez‐Ruiz, L., Martínez-Morcillo, F. J., Alcaraz‐Pérez, F., Martínez-Navarro, F. J., Lachaud, C., Ahmed, N., Schroeder, T., Pardo-Sánchez, I., et al. (2019) · Immunity · doi:10.1016/j.immuni.2019.05.005 · Cited by 85 · see citing works
Cunha, L. D., Silva, A. L. N., Ribeiro, J. M., Mascarenhas, D. P. A., Quirino, G. F. S., dos Santos, L. L., Flavell, R. A., & Zamboni, D. S. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.086 · Cited by 84 · see citing works
Webster, S. J., Brode, S., Ellis, L., Fitzmaurice, T. J., Elder, M. J., Gekara, N. O., Tourlomousis, P., Bryant, C. E., Clare, S., Chee, R., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006383 · Cited by 81 · see citing works
Yi, Y. (2019) · Immunology · doi:10.1111/imm.13134 · Cited by 81 · see citing works
Pyroptosis and respiratory diseases: A review of current knowledge
Sun, J., & Li, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.920464 · Cited by 82 · see citing works
Naseer, N., Egan, M. S., Ruiz, V. M. R., Scott, W. P., Hunter, E. N., Demissie, T., Rauch, I., Brodsky, I. E., & Shin, S. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1009718 · Cited by 83 · see citing works
Dickinson, M. S., Kutsch, M., Sistemich, L., Hernandez, D., Piro, A. S., Needham, D., Lesser, C. F., Herrmann, C., & Coers, J. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2216028120 · Cited by 76 · see citing works
Self-citationInterferons and inflammasomes: Cooperation and counterregulation in disease
Labzin, L. I., Lauterbach, M., & Latz, E. (2016) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2016.05.010 · Cited by 76 · see citing works
Human GBP1 does not localize to pathogen vacuoles but restrictsToxoplasma gondii
Johnston, A. C., Piro, A. L., Clough, B., Siew, M., Winter, S. V., Coers, J., & Frickel, E. (2016) · Cellular Microbiology · doi:10.1111/cmi.12579 · Cited by 78 · see citing works
Self-citationMechanisms and Consequences of Noncanonical Inflammasome-Mediated Pyroptosis
Wright, S. S., Vasudevan, S. O., & Rathinam, V. A. K. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167245 · Cited by 74 · see citing works
Cerqueira, D. M., Pereira, M. S. F., Silva, A. L. N., Cunha, L. D., & Zamboni, D. S. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1501223 · Cited by 76 · see citing works
The Inflammatory Caspases-1 and -11 Mediate the Pathogenesis of Dermatitis in Sharpin-Deficient Mice
Douglas, T., Champagne, C., Morizot, A., Lapointe, J., & Saleh, M. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500542 · Cited by 74 · see citing works
Diverse mechanisms for inflammasome sensing of cytosolic bacteria and bacterial virulence
Zhao, Y., & Shao, F. (2016) · Current Opinion in Microbiology · doi:10.1016/j.mib.2015.10.003 · Cited by 73 · see citing works
Wang, X., Ni, J., You, Y., Feng, G., Zhang, S., Bao, W., Hou, H., Li, H., Liu, L., Zheng, M., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108080 · Cited by 71 · see citing works
Caspase‐11: arming the guards against bacterial infection
Stowe, I. B., Lee, B. L., & Kayagaki, N. (2015) · Immunological Reviews · doi:10.1111/imr.12292 · Cited by 73 · see citing works
The nucleic acid‐sensing inflammasomes
Xiao, T. S. (2015) · Immunological Reviews · doi:10.1111/imr.12281 · Cited by 68 · see citing works
- Authors
- 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.
- Affiliations
- Duke University (US)
- University of North Carolina at Chapel Hill (US)
- University of Maryland, Baltimore (US)
- Heinrich Heine University Düsseldorf (DE)
- The University of Osaka (JP)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-04-08
- Volume
- 111
- Issue
- 16
- Pages
- 6046-6051
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4000848
- OpenAlex
- W1984035213
- Cited by
- 357
- References
- 43
- Citations by year
- 2026: 20 · 2025: 28 · 2024: 24 · 2023: 27 · 2022: 32 · 2021: 22 · 2020: 42 · 2019: 32 · 2018: 26 · 2017: 30 · 2016: 31 · 2015: 31 · 2014: 11
- FWCI
- 14.07
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association (12PRE10440003)
- Deutsche Forschungsgemeinschaft (FOR729)
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (R21AI099823, R01AI103197, R01AI097518, U54AI057157, R37AI103197)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- guanylate-binding proteins, caspase-11, pyroptosis, non-canonical inflammasome, Legionella pneumophila, cell-autonomous immunity, macrophages, interferon signaling, Escherichia coli LPS, intracellular bacterial infection
- MeSH terms
- NADPH Oxidase 2, Animals, Cytoplasm, Enzyme Activation, Interferon-gamma, Legionnaires' Disease, Lipopolysaccharides, Macrophage Activation, Macrophages, Membrane Glycoproteins, Mice, Inbred C57BL, Mutation, Salmonella typhimurium, Legionella pneumophila, Apoptosis, GTP-Binding Proteins, NADPH Oxidases, Caspases, Mice, Nitric Oxide Synthase Type II, Caspases, Initiator
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