{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T04:01:41Z","timestamp":1793246501605,"version":"4.5.0"},"reference-count":34,"publisher":"National Academy of Sciences","issue":"16","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2014,4,22]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    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\n                    <jats:italic>Legionella<\/jats:italic>\n                    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.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1321700111","type":"journal-article","created":{"date-parts":[[2014,4,9]],"date-time":"2014-04-09T02:59:49Z","timestamp":1397012389000},"page":"6046-6051","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":365,"title":["Guanylate binding proteins promote caspase-11\u2013dependent pyroptosis in response to cytoplasmic LPS"],"prefix":"10.1073","volume":"111","author":[{"given":"Danielle M.","family":"Pilla","sequence":"first","affiliation":[{"name":"Departments of Molecular Genetics and Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jon A.","family":"Hagar","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arun K.","family":"Haldar","sequence":"additional","affiliation":[{"name":"Departments of Molecular Genetics and Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ashley K.","family":"Mason","sequence":"additional","affiliation":[{"name":"Department of Microbial Pathogenesis, School of Dentistry, University of Maryland, Baltimore, MD 21203;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Degrandi","sequence":"additional","affiliation":[{"name":"Institute of Medical Microbiology and Hospital Hygiene, Heinrich Heine University Duesseldorf, Duesseldorf 40225, Germany; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Klaus","family":"Pfeffer","sequence":"additional","affiliation":[{"name":"Institute of Medical 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