{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T00:02:27Z","timestamp":1791158547151,"version":"4.1.0"},"reference-count":67,"publisher":"American Society for Microbiology","issue":"21","license":[{"start":{"date-parts":[[2014,11,1]],"date-time":"2014-11-01T00:00:00Z","timestamp":1414800000000},"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":["J Bacteriol"],"published-print":{"date-parts":[[2014,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Listeria monocytogenes<\/jats:named-content>\n                    is a Gram-positive facultative intracellular pathogen that is highly resistant to lysozyme, a ubiquitous enzyme of the innate immune system that degrades cell wall peptidoglycan. Two peptidoglycan-modifying enzymes, PgdA and OatA, confer lysozyme resistance on\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">L. monocytogenes<\/jats:named-content>\n                    ; however, these enzymes are also conserved among lysozyme-sensitive nonpathogens. We sought to identify additional factors responsible for lysozyme resistance in\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">L. monocytogenes<\/jats:named-content>\n                    . A forward genetic screen for lysozyme-sensitive mutants led to the identification of 174 transposon insertion mutations that mapped to 13 individual genes. Four mutants were killed exclusively by lysozyme and not other cell wall-targeting molecules, including the peptidoglycan deacetylase encoded by\n                    <jats:italic>pgdA<\/jats:italic>\n                    , the putative carboxypeptidase encoded by\n                    <jats:italic>pbpX<\/jats:italic>\n                    , the orphan response regulator encoded by\n                    <jats:italic>degU<\/jats:italic>\n                    , and the highly abundant noncoding RNA encoded by\n                    <jats:italic>rli31<\/jats:italic>\n                    . Both\n                    <jats:italic>degU<\/jats:italic>\n                    and\n                    <jats:italic>rli31<\/jats:italic>\n                    mutants had reduced expression of\n                    <jats:italic>pbpX<\/jats:italic>\n                    and\n                    <jats:italic>pgdA<\/jats:italic>\n                    , yet DegU and Rli31 did not regulate each other. Since\n                    <jats:italic>pbpX<\/jats:italic>\n                    and\n                    <jats:italic>pgdA<\/jats:italic>\n                    are also present in lysozyme-sensitive bacteria, this suggested that the acquisition of novel enzymes was not responsible for lysozyme resistance, but rather, the regulation of conserved enzymes by DegU and Rli31 conferred high lysozyme resistance. Each lysozyme-sensitive mutant exhibited attenuated virulence in mice, and a time course of infection revealed that the most lysozyme-sensitive strain was killed within 30 min of intravenous infection, a phenotype that was recapitulated in purified blood. Collectively, these data indicate that the genes required for lysozyme resistance are highly upregulated determinants of\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">L. monocytogenes<\/jats:named-content>\n                    pathogenesis that are required for avoiding the enzymatic activity of lysozyme in the blood.\n                  <\/jats:p>","DOI":"10.1128\/jb.02053-14","type":"journal-article","created":{"date-parts":[[2014,8,26]],"date-time":"2014-08-26T00:40:32Z","timestamp":1409013632000},"page":"3756-3767","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":70,"title":["Listeria monocytogenes Is Resistant to Lysozyme through the Regulation, Not the Acquisition, of Cell Wall-Modifying Enzymes"],"prefix":"10.1128","volume":"196","author":[{"given":"Thomas P.","family":"Burke","sequence":"first","affiliation":[{"name":"Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anastasia","family":"Loukitcheva","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jason","family":"Zemansky","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard","family":"Wheeler","sequence":"additional","affiliation":[{"name":"Institut Pasteur, Biology and Genetics of the Bacterial Cell Wall Unit, Paris, France"},{"name":"INSERM, Aveny Group, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ivo G.","family":"Boneca","sequence":"additional","affiliation":[{"name":"Institut Pasteur, Biology and Genetics of the Bacterial Cell Wall Unit, Paris, France"},{"name":"INSERM, Aveny Group, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel A.","family":"Portnoy","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA"},{"name":"School of Public Health, University of California, Berkeley, Berkeley, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1007\/s12038-010-0015-5"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.139.5.1228"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0009-8981(74)90398-2"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2007.00099.x"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00651-10"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2007.00088.x"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M910189199"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2004.04446.x"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0609672104"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00077-11"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.14.3.584-640.2001"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1093\/infdis\/jir396"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.06023-11"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00301-06"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/0300-9084(92)90143-3"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.184.15.4177-4186.2002"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1993.tb01211.x"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2000.01643.x"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1038\/nmeth.1923"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1093\/bioinformatics\/btp352"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.C200651200"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M304749200"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00016-09"},{"key":"e_1_3_3_25_2","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1111\/j.1755-3768.1984.tb08445.x","article-title":"Lysozyme concentration in tears\u2014assessment of reference values in normal subjects","volume":"62","author":"Aine E","year":"1984","unstructured":"AineEMorskyP. 1984. 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