{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T02:53:20Z","timestamp":1792205600747,"version":"4.4.0"},"reference-count":73,"publisher":"National Academy of Sciences","issue":"23","license":[{"start":{"date-parts":[[2023,5,30]],"date-time":"2023-05-30T00:00:00Z","timestamp":1685404800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["AI119580-01"],"award-info":[{"award-number":["AI119580-01"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2023,6,6]]},"abstract":"<jats:p>\n                    Peptidoglycan is a critical component of the bacteria cell envelope. Remodeling of the peptidoglycan is required for numerous essential cellular processes and has been linked to bacterial pathogenesis. Peptidoglycan deacetylases that remove the acetyl group of the\n                    <jats:italic>N<\/jats:italic>\n                    -acetylglucosamine (NAG) subunit protect bacterial pathogens from immune recognition and digestive enzymes secreted at the site of infection. However, the full extent of this modification on bacterial physiology and pathogenesis is not known. Here, we identify a polysaccharide deacetylase of the intracellular bacterial pathogen\n                    <jats:italic>Legionella pneumophila<\/jats:italic>\n                    and define a two-tiered role for this enzyme in\n                    <jats:italic>Legionella<\/jats:italic>\n                    pathogenesis. First, NAG deacetylation is important for the proper localization and function of the Type IVb secretion system, linking peptidoglycan editing to the modulation of host cellular processes through the action of secreted virulence factors. As a consequence, the\n                    <jats:italic>Legionella<\/jats:italic>\n                    vacuole mis-traffics along the endocytic pathway to the lysosome, preventing the formation of a replication permissive compartment. Second, within the lysosome, the inability to deacetylate the peptidoglycan renders the bacteria more sensitive to lysozyme-mediated degradation, resulting in increased bacterial death. Thus, the ability to deacetylate NAG is important for bacteria to persist within host cells and in turn,\n                    <jats:italic>Legionella<\/jats:italic>\n                    virulence. Collectively, these results expand the function of peptidoglycan deacetylases in bacteria, linking peptidoglycan editing, Type IV secretion, and the intracellular fate of a bacterial pathogen.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2119658120","type":"journal-article","created":{"date-parts":[[2023,5,30]],"date-time":"2023-05-30T13:31:38Z","timestamp":1685453498000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":21,"title":["Peptidoglycan deacetylation controls type IV secretion and the intracellular survival of the bacterial pathogen\n                    <i>Legionella pneumophila<\/i>"],"prefix":"10.1073","volume":"120","author":[{"given":"David","family":"Boamah","sequence":"first","affiliation":[{"name":"Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6848-5134","authenticated-orcid":false,"given":"Michael\u00a0C.","family":"Gilmore","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology, Laboratory for Molecular Infection Medicine Sweden, Ume\u00e5 Centre for Microbial Research, Ume\u00e5 University, Ume\u00e5 90187, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah","family":"Bourget","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6699-7737","authenticated-orcid":false,"given":"Anushka","family":"Ghosh","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohammad\u00a0J.","family":"Hossain","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph\u00a0P.","family":"Vogel","sequence":"additional","affiliation":[{"name":"Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5995-718X","authenticated-orcid":false,"given":"Felipe","family":"Cava","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology, Laboratory for Molecular Infection Medicine Sweden, Ume\u00e5 Centre for Microbial Research, Ume\u00e5 University, Ume\u00e5 90187, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tamara\u00a0J.","family":"O\u2019Connor","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2023,5,30]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2007.00094.x"},{"key":"e_1_3_4_2_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2008.00102.x"},{"key":"e_1_3_4_3_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.26.15405"},{"key":"e_1_3_4_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.184.21.6007-6015.2002"},{"key":"e_1_3_4_5_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.RA118.004273"},{"key":"e_1_3_4_6_2","doi-asserted-by":"publisher","DOI":"10.1111\/mmi.12137"},{"key":"e_1_3_4_7_2","doi-asserted-by":"publisher","DOI":"10.1099\/mic.0.28141-0"},{"key":"e_1_3_4_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00480-07"},{"key":"e_1_3_4_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41564-018-0248-x"},{"key":"e_1_3_4_10_2","doi-asserted-by":"publisher","DOI":"10.15252\/embr.201643206"},{"key":"e_1_3_4_11_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2002.tb00599.x"},{"key":"e_1_3_4_12_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.90.2.625"},{"key":"e_1_3_4_13_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF00294524"},{"key":"e_1_3_4_14_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M910189199"},{"key":"e_1_3_4_15_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.70.12.7176-7178.2002"},{"key":"e_1_3_4_16_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0609672104"},{"key":"e_1_3_4_17_2","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.00409-12"},{"key":"e_1_3_4_18_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI57761"},{"key":"e_1_3_4_19_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2008.06463.x"},{"key":"e_1_3_4_20_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00651-10"},{"key":"e_1_3_4_21_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.158.4.1319"},{"key":"e_1_3_4_22_2","doi-asserted-by":"publisher","DOI":"10.1128\/aem.41.1.9-16.1981"},{"key":"e_1_3_4_23_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijheh.2017.10.011"},{"key":"e_1_3_4_24_2","doi-asserted-by":"publisher","DOI":"10.3389\/fcimb.2017.00477"},{"key":"e_1_3_4_25_2","doi-asserted-by":"publisher","DOI":"10.1086\/498575"},{"key":"e_1_3_4_26_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI110744"},{"key":"e_1_3_4_27_2","first-page":"206","article-title":"The 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