{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T10:38:44Z","timestamp":1785580724203,"version":"3.56.0"},"reference-count":45,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2020,7,23]],"date-time":"2020-07-23T00:00:00Z","timestamp":1595462400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Immunology"],"published-print":{"date-parts":[[2020,10]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Interleukin\u20101<jats:italic>\u03b2<\/jats:italic> (IL\u20101<jats:italic>\u03b2<\/jats:italic>) plays pivotal roles in controlling bacterial infections and is produced after the processing of pro\u2010IL\u20101<jats:italic>\u03b2<\/jats:italic> by caspase\u20101, which is activated by the inflammasome. In addition, caspase\u20101 cleaves the cytosolic protein, gasdermin\u2010D (GSDMD), whose N\u2010terminal fragment subsequently forms a pore in the plasma membrane, leading to the pyroptic cell\u2010death\u2010mediated release of IL\u20101<jats:italic>\u03b2<\/jats:italic>. Living cells can also release IL\u20101<jats:italic>\u03b2<\/jats:italic> via GSDMD pores or other unconventional secretory pathways. However, the precise mechanisms are poorly defined. Here, we show that lipoproteins from <jats:italic>Mycoplasma salivarium<\/jats:italic> (MsLP) and <jats:italic>Mycoplasma pneumoniae<\/jats:italic> (MpLP) and an <jats:italic>M.\u00a0salivarium<\/jats:italic>\u2010derived lipopeptide (FSL\u20101), which are activators of the nucleotide\u2010binding oligomerization domain\u2010like receptor family, pyrin domain containing 3 (NLRP3) inflammasome, induce IL\u20101<jats:italic>\u03b2<\/jats:italic> release from mouse bone\u2010marrow\u2010derived macrophages (BMMs) without inducing cell death. The levels of IL\u20101<jats:italic>\u03b2<\/jats:italic> release induced by MsLP, MpLP and FSL\u20101 were more than 100 times lower than those induced by the canonical NLRP3 activator nigericin. The IL\u20101<jats:italic>\u03b2<\/jats:italic> release\u2010inducing activities of MsLP, MpLP and FSL\u20101 were not attenuated in BMMs from GSDMD\u2010deficient mice. Furthermore, both active caspase\u20101 and cleaved GSDMD were detected in response to transfection of FSL\u20101 into the cytosol of BMMs, but the release of IL\u20101<jats:italic>\u03b2<\/jats:italic> was unaffected by GSDMD deficiency. Meanwhile, punicalagin, a membrane\u2010stabilizing agent, drastically down\u2010regulated the release of IL\u20101<jats:italic>\u03b2<\/jats:italic> in response to FSL\u20101. These results suggest that mycoplasmal lipoprotein\/lipopeptide\u2010induced IL\u20101<jats:italic>\u03b2<\/jats:italic> release by living macrophages is not mediated via GSDMD but rather through changes in membrane permeability.<\/jats:p>","DOI":"10.1111\/imm.13230","type":"journal-article","created":{"date-parts":[[2020,6,27]],"date-time":"2020-06-27T10:23:42Z","timestamp":1593253422000},"page":"114-122","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["Gasdermin D\u2010independent release of interleukin\u20101<i>\u03b2<\/i> by living macrophages in response to mycoplasmal lipoproteins and lipopeptides"],"prefix":"10.1111","volume":"161","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0149-7181","authenticated-orcid":false,"given":"Ayumi","family":"Saeki","sequence":"first","affiliation":[{"name":"Department of Oral Molecular Microbiology Faculty of Dental Medicine and Graduate School of Dental Medicine Hokkaido University Sapporo Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kohsuke","family":"Tsuchiya","sequence":"additional","affiliation":[{"name":"Division of Immunology and Molecular Biology Cancer Research Institute Kanazawa University Kanazawa Japan"},{"name":"Institute for Frontier Science Initiative (InFiniti) Kanazawa University Kanazawa Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takashi","family":"Suda","sequence":"additional","affiliation":[{"name":"Division of Immunology and Molecular Biology Cancer Research Institute Kanazawa University Kanazawa Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takeshi","family":"Into","sequence":"additional","affiliation":[{"name":"Department of Oral Microbiology Division of Oral Infections and Health Sciences Asahi University School of Dentistry Hozumi Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akira","family":"Hasebe","sequence":"additional","affiliation":[{"name":"Department of Oral Molecular Microbiology Faculty of Dental Medicine and Graduate School of Dental Medicine Hokkaido University Sapporo Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Toshihiko","family":"Suzuki","sequence":"additional","affiliation":[{"name":"Department of Bacterial Pathogenesis, Infection and Host Response Graduate School of Medical and Dental Sciences Tokyo Medical and Dental University Bunkyo\u2010ku Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6497-9073","authenticated-orcid":false,"given":"Ken\u2010ichiro","family":"Shibata","sequence":"additional","affiliation":[{"name":"Department of Oral Molecular Microbiology Faculty of Dental Medicine and Graduate School of Dental Medicine Hokkaido University Sapporo 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