{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T19:32:53Z","timestamp":1791142373417,"version":"4.1.0"},"reference-count":49,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[2009,3,1]],"date-time":"2009-03-01T00:00:00Z","timestamp":1235865600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2009,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>Multiple microbial components trigger the formation of an inflammasome complex that contains pathogen-specific nucleotide oligomerization and binding domain (NOD)-like receptors (NLRs), caspase-1, and in some cases the scaffolding protein ASC. The NLR protein Nalp1b has been linked to anthrax lethal toxin (LT)-mediated cytolysis of murine macrophages. Here we demonstrate that in unstimulated J774A.1 macrophages, caspase-1 and Nalp1b are membrane associated and part of \u223c200- and \u223c800-kDa complexes, respectively. LT treatment of these cells resulted in caspase-1 recruitment to the Nalp1b-containing complex, concurrent with processing of cytosolic caspase-1 substrates. We further demonstrated that Nalp1b and caspase-1 are able to interact with each other. Intriguingly, both caspase-1 and Nalp1b were membrane associated, while the caspase-1 substrate interleukin-18 was cytosolic. Caspase-1-associated inflammasome components included, besides Nalp1b, proinflammatory caspase-11 and the caspase-1 substrate \u03b1-enolase. Asc was not part of the Nalp1b inflammasome in LT-treated macrophages. Taken together, our findings suggest that LT triggers the formation of a membrane-associated inflammasome complex in murine macrophages, resulting in cleavage of cytosolic caspase-1 substrates and cell death.<\/jats:p>","DOI":"10.1128\/iai.01032-08","type":"journal-article","created":{"date-parts":[[2009,1,5]],"date-time":"2009-01-05T20:34:03Z","timestamp":1231187643000},"page":"1262-1271","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":70,"title":["Anthrax Lethal Toxin Triggers the Formation of a Membrane-Associated Inflammasome Complex in Murine Macrophages"],"prefix":"10.1128","volume":"77","author":[{"given":"Adel M.","family":"Nour","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yee-Guide","family":"Yeung","sequence":"additional","affiliation":[{"name":"Department of Developmental and Molecular Biology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura","family":"Santambrogio","sequence":"additional","affiliation":[{"name":"Department of Pathology, Albert Einstein College of Medicine, Bronx, New York 10461"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eric D.","family":"Boyden","sequence":"additional","affiliation":[{"name":"Department of Orthopedics, Children's Hospital Boston, Boston, Massachusetts 02115"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"E. Richard","family":"Stanley","sequence":"additional","affiliation":[{"name":"Department of Developmental and Molecular Biology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ju\u0308rgen","family":"Brojatsch","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1074-7613(04)00046-9"},{"key":"e_1_3_2_3_2","unstructured":"Protein localization by fluorescence microscopy. 2002"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1055\/s-0038-1657693"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200502153"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/35019501"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng1724"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.275.9.6067"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M107419200"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81417-8"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.cellbio.19.111301.140655"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2006.00751.x"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2007.01036.x"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1086\/317604"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(00)02015-9"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.3.11.1269"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.74.082803.133347"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.cdd.4401087"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.immuni.2007.03.008"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M306162200"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1994.tb00500.x"},{"key":"e_1_3_2_22_2","first-page":"477","volume":"10","year":"2008","unstructured":"Kufer, T. 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