{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T02:33:20Z","timestamp":1773282800439,"version":"3.50.1"},"update-to":[{"DOI":"10.1371\/journal.ppat.1011047","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2023,2,14]],"date-time":"2023-02-14T00:00:00Z","timestamp":1676332800000}}],"reference-count":63,"publisher":"Public Library of Science (PLoS)","issue":"2","license":[{"start":{"date-parts":[[2023,2,2]],"date-time":"2023-02-02T00:00:00Z","timestamp":1675296000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["398967434 \u2014TRR261"],"award-info":[{"award-number":["398967434 \u2014TRR261"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["390536577"],"award-info":[{"award-number":["390536577"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"name":"BONFOR"},{"DOI":"10.13039\/100010127","name":"J\u00fcrgen Manchot Stiftung","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010127","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010127","name":"J\u00fcrgen Manchot Stiftung","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010127","id-type":"DOI","asserted-by":"publisher"}]},{"name":"FemHabil"},{"DOI":"10.13039\/501100007601","name":"Horizon 2020","doi-asserted-by":"publisher","award":["721484"],"award-info":[{"award-number":["721484"]}],"id":[{"id":"10.13039\/501100007601","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["1R35GM124798"],"award-info":[{"award-number":["1R35GM124798"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    The obligate intracellular\n                    <jats:italic>Chlamydiaceae<\/jats:italic>\n                    do not need to resist osmotic challenges and thus lost their cell wall in the course of evolution. Nevertheless, these pathogens maintain a rudimentary peptidoglycan machinery for cell division. They build a transient peptidoglycan ring, which is remodeled during the process of cell division and degraded afterwards. Uncontrolled degradation of peptidoglycan poses risks to the chlamydial cell, as essential building blocks might get lost or trigger host immune response upon release into the host cell. Here, we provide evidence that a primordial enzyme class prevents energy intensive\n                    <jats:italic>de novo<\/jats:italic>\n                    synthesis and uncontrolled release of immunogenic peptidoglycan subunits in\n                    <jats:italic>Chlamydia trachomatis<\/jats:italic>\n                    . Our data indicate that the homolog of a\n                    <jats:italic>Bacillus<\/jats:italic>\n                    NlpC\/P60 protein is widely conserved among\n                    <jats:italic>Chlamydiales<\/jats:italic>\n                    . We show that the enzyme is tailored to hydrolyze peptidoglycan-derived peptides, does not interfere with peptidoglycan precursor biosynthesis, and is targeted by cysteine protease inhibitors\n                    <jats:italic>in vitro<\/jats:italic>\n                    and in cell culture. The peptidase plays a key role in the underexplored process of chlamydial peptidoglycan recycling. Our study suggests that chlamydiae orchestrate a closed-loop system of peptidoglycan ring biosynthesis, remodeling, and recycling to support cell division and maintain long-term residence inside the host. Operating at the intersection of energy recovery, cell division and immune evasion, the peptidoglycan recycling NlpC\/P60 peptidase could be a promising target for the development of drugs that combine features of classical antibiotics and anti-virulence drugs.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1011047","type":"journal-article","created":{"date-parts":[[2023,2,2]],"date-time":"2023-02-02T14:41:12Z","timestamp":1675348872000},"page":"e1011047","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":20,"title":["An NlpC\/P60 protein catalyzes a key step in peptidoglycan recycling at the intersection of energy recovery, cell division and immune evasion in the intracellular pathogen Chlamydia trachomatis"],"prefix":"10.1371","volume":"19","author":[{"given":"Jula","family":"Reuter","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christian","family":"Otten","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nicolas","family":"Jacquier","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Junghoon","family":"Lee","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dominique","family":"Mengin-Lecreulx","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Iris","family":"L\u00f6ckener","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert","family":"Kluj","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christoph","family":"Mayer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Federico","family":"Corona","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Julia","family":"Dannenberg","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S\u00e9bastien","family":"Aeby","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Henrike","family":"B\u00fchl","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gilbert","family":"Greub","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Waldemar","family":"Vollmer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Scot 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Jacquier","year":"2015","journal-title":"FEMS Microbiol Rev"},{"key":"ppat.1011047.ref003","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1111\/mmi.13880","article-title":"Peptidoglycan in obligate intracellular bacteria","volume":"107","author":"C Otten","year":"2018","journal-title":"Mol Microbiol"},{"key":"ppat.1011047.ref004","first-page":"1","article-title":"Deconstructing the chlamydial cell wall","volume":"412","author":"A Kl\u00f6ckner","year":"2018","journal-title":"Curr Top Microbiol Immunol"},{"key":"ppat.1011047.ref005","first-page":"12","article-title":"Pathogenic Chlamydia Lack a Classical Sacculus but Synthesize a Narrow, Mid-cell Peptidoglycan Ring, Regulated by MreB, for Cell Division.","author":"G Liechti","year":"2016","journal-title":"PLoS Pathog"},{"key":"ppat.1011047.ref006","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/nature12892","article-title":"A new metabolic cell-wall labelling method reveals peptidoglycan in Chlamydia 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Atwal","year":"2021","journal-title":"mBio"},{"key":"ppat.1011047.ref020","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/ncomms5201","article-title":"AmiA is a penicillin target enzyme with dual activity in the intracellular pathogen Chlamydia pneumoniae","volume":"5","author":"A Kl\u00f6ckner","year":"2014","journal-title":"Nat Commun"},{"key":"ppat.1011047.ref021","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1016\/j.chembiol.2015.08.009","article-title":"Disassembly of a Medial Transenvelope Structure by Antibiotics during Intracellular Division","volume":"22","author":"N Jacquier","year":"2015","journal-title":"Chem Biol"},{"key":"ppat.1011047.ref022","doi-asserted-by":"crossref","first-page":"e1005822","DOI":"10.1371\/journal.ppat.1005822","article-title":"Polarized Cell Division of Chlamydia trachomatis","volume":"12","author":"Y Abdelrahman","year":"2016","journal-title":"PLoS 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Reviews"},{"key":"ppat.1011047.ref026","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1128\/JB.180.5.1215-1223.1998","article-title":"MppA, a periplasmic binding protein essential for import of the bacterial cell wall peptide L-alanyl-\u03b3-D-glutamyl-meso-diaminopimelate","volume":"180","author":"JT Park","year":"1998","journal-title":"J Bacteriol"},{"key":"ppat.1011047.ref027","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1111\/j.1749-6632.2012.06813.x","article-title":"Bacterial cell-wall recycling","volume":"1277","author":"JW Johnson","year":"2013","journal-title":"Ann N Y Acad Sci"},{"key":"ppat.1011047.ref028","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/bs.aambs.2020.04.001","article-title":"Peptidoglycan biosynthesis and remodeling revisited","volume":"112","author":"M Shaku","year":"2020","journal-title":"Adv Appl Microbiol"},{"key":"ppat.1011047.ref029","doi-asserted-by":"crossref","first-page":"e01128","DOI":"10.1128\/mBio.01128-19","article-title":"A spoiid homolog cleaves glycan strands at the chlamydial division septum.","volume":"10","author":"N Jacquier","year":"2019","journal-title":"mBio"},{"key":"ppat.1011047.ref030","doi-asserted-by":"crossref","first-page":"e00086","DOI":"10.1128\/IAI.00086-20","article-title":"Chlamydia trachomatis Oligopeptide Transporter Performs Dual Functions of Oligopeptide Transport and Peptidoglycan Recycling","volume":"88","author":"R Singh","year":"2020","journal-title":"Infect Immun"},{"key":"ppat.1011047.ref031","doi-asserted-by":"crossref","first-page":"1354","DOI":"10.1107\/S1744309110021214","article-title":"Structure of the \u03b3-D-glutamyl-L-diamino acid endopeptidase YkfC from Bacillus cereus in complex with L-Ala-\u03b3-d-Glu: Insights into substrate recognition by NlpC\/P60 cysteine peptidases","volume":"66","author":"Q Xu","year":"2010","journal-title":"Acta Crystallogr Sect F Struct Biol Cryst Commun"},{"key":"ppat.1011047.ref032","article-title":"Insights into substrate specificity of NlpC\/P60 cell wall hydrolases containing bacterial SH3 domains.","volume":"6","author":"Q Xu","year":"2015","journal-title":"mBio"},{"key":"ppat.1011047.ref033","doi-asserted-by":"crossref","first-page":"1036","DOI":"10.1111\/mmi.12058","article-title":"Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12","volume":"86","author":"SK Singh","year":"2012","journal-title":"Mol Microbiol"},{"key":"ppat.1011047.ref034","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1089\/mdr.1996.2.63","article-title":"Overproduction of Penicillin-Binding Protein 7 Suppresses Thermosensitive Growth Defect at Low Osmolarity due to an spr Mutation of Escherichia coli","volume":"2","author":"H Hara","year":"1996","journal-title":"Microbial Drug 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Hydrolases.","volume":"9","author":"J Pinheiro","year":"2018","journal-title":"mBio"},{"key":"ppat.1011047.ref045","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1111\/j.1574-6968.1993.tb06189.x","article-title":"Description and partial characterization of a new Chlamydia-like microorganism","volume":"109","author":"S Kahane","year":"1993","journal-title":"FEMS Microbiol Lett"},{"key":"ppat.1011047.ref046","first-page":"4","article-title":"Discovery of chlamydial peptidoglycan reveals bacteria with murein sacculi but without FtsZ.","author":"M Pilhofer","year":"2013","journal-title":"Nat Commun."},{"key":"ppat.1011047.ref047","first-page":"87","article-title":"Why is Chlamydia sensitive to penicillin in the absence of peptidoglycan?","volume":"2","author":"JW Moulder","year":"1993","journal-title":"Infect Agents Dis."},{"key":"ppat.1011047.ref048","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.tim.2005.12.004","article-title":"Building the invisible wall: updating the chlamydial peptidoglycan anomaly","volume":"14","author":"AJ McCoy","year":"2006","journal-title":"Trends Microbiol"},{"key":"ppat.1011047.ref049","doi-asserted-by":"crossref","first-page":"e7723","DOI":"10.1371\/journal.pone.0007723","article-title":"Penicillin induced persistence in Chlamydia trachomatis: high quality time lapse video analysis of the developmental cycle.","volume":"4","author":"RJ Skilton","year":"2009","journal-title":"PLoS One"},{"key":"ppat.1011047.ref050","doi-asserted-by":"crossref","first-page":"15707","DOI":"10.1021\/bi011640x","article-title":"Evolution of enzymatic activities in the enolase superfamily: functional assignment of unknown proteins in Bacillus subtilis and Escherichia coli as L-Ala-D\/L-Glu epimerases","volume":"40","author":"DM Schmidt","year":"2001","journal-title":"Biochemistry"},{"key":"ppat.1011047.ref051","doi-asserted-by":"crossref","first-page":"1911","DOI":"10.1128\/JB.185.6.1911-1922.2003","article-title":"Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis","volume":"185","author":"V Molle","year":"2003","journal-title":"J Bacteriol"},{"key":"ppat.1011047.ref052","doi-asserted-by":"crossref","first-page":"1390","DOI":"10.1038\/s41564-020-0762-5","article-title":"Reprogramming of host glutamine metabolism during Chlamydia trachomatis infection and its key role in peptidoglycan synthesis","volume":"5","author":"K Rajeeve","year":"2020","journal-title":"Nat Microbiol"},{"key":"ppat.1011047.ref053","doi-asserted-by":"crossref","first-page":"17909","DOI":"10.1073\/pnas.0608643103","article-title":"L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate\/lysine","volume":"103","author":"AJ McCoy","year":"2006","journal-title":"Proc Natl Acad Sci U S 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