{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T05:05:32Z","timestamp":1788930332730,"version":"build-2803163510"},"update-to":[{"DOI":"10.1371\/journal.ppat.1013633","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T00:00:00Z","timestamp":1761609600000}}],"reference-count":56,"publisher":"Public Library of Science (PLoS)","issue":"10","license":[{"start":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T00:00:00Z","timestamp":1761004800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001711","name":"Schweizerischer Nationalfonds zur F\u00c3\u00b6rderung der Wissenschaftlichen Forschung","doi-asserted-by":"publisher","award":["PR00P3_185713"],"award-info":[{"award-number":["PR00P3_185713"]}],"id":[{"id":"10.13039\/501100001711","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Cystische Fibrose Schweiz","award":["\/"],"award-info":[{"award-number":["\/"]}]},{"DOI":"10.13039\/501100023177","name":"Fondation Pierre Mercier pour la Science","doi-asserted-by":"publisher","award":["\/"],"award-info":[{"award-number":["\/"]}],"id":[{"id":"10.13039\/501100023177","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100022796","name":"Jubil\u00c3\u00a4umsstiftung von Swiss Life","doi-asserted-by":"publisher","award":["\/"],"award-info":[{"award-number":["\/"]}],"id":[{"id":"10.13039\/501100022796","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"crossref","award":["VR2018-02823"],"award-info":[{"award-number":["VR2018-02823"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100004063","name":"Knut och Alice Wallenbergs Stiftelse","doi-asserted-by":"publisher","award":["KAW2012.0184"],"award-info":[{"award-number":["KAW2012.0184"]}],"id":[{"id":"10.13039\/501100004063","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100016756","name":"Kempe Foundation","doi-asserted-by":"publisher","award":["SMK2062"],"award-info":[{"award-number":["SMK2062"]}],"id":[{"id":"10.13039\/100016756","id-type":"DOI","asserted-by":"publisher"}]},{"name":"The Laboratory of Molecular Infection Medicine Sweden (MIMS) Cancerfonden","award":["\/"],"award-info":[{"award-number":["\/"]}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    Beta-lactam antibiotics are widely used to treat bacterial infections, but their efficacy is compromised by resistance mechanisms such as the production of beta-lactamases. In\n                    <jats:italic>\n                      <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n                    <\/jats:italic>\n                    , the chromosomally encoded beta-lactamase AmpC is the primary mediator of beta-lactam resistance.\n                    <jats:italic>\n                      <jats:italic>ampC<\/jats:italic>\n                    <\/jats:italic>\n                    expression is regulated by the transcription factor AmpR, which responds to intracellular peptidoglycan (PG) fragments. Under normal conditions, AmpR binds the PG precursor (UDP-MurNAc-pentapeptide) and represses\n                    <jats:italic>\n                      <jats:italic>ampC<\/jats:italic>\n                    <\/jats:italic>\n                    expression. However, during beta-lactam treatment or in PG recycling-deficient mutants such as\n                    <jats:italic>\n                      <jats:italic>ampD<\/jats:italic>\n                    <\/jats:italic>\n                    mutants, PG degradation products (anhydromuropeptides) accumulate and activate AmpR, resulting in elevated\n                    <jats:italic>\n                      <jats:italic>ampC<\/jats:italic>\n                    <\/jats:italic>\n                    expression and beta-lactam resistance. We hypothesized that shifting the balance of PG precursors could modulate AmpR activity and suppress beta-lactamase expression, even in derepressed strains. Undecaprenyl phosphate (UndP) is a lipid carrier essential for translocating PG precursors across the bacterial inner membrane. Recent work has identified members of the DedA superfamily as UndP flippases responsible for recycling this lipid carrier. Disruption of UndP recycling leads to cytoplasmic accumulation of UDP-MurNAc-pentapeptide, the known AmpR repressor. Here, we show that deletion of\n                    <jats:italic>\n                      <jats:italic>dedA4<\/jats:italic>\n                    <\/jats:italic>\n                    , which encodes a predicted UndP flippase in\n                    <jats:italic>\n                      <jats:italic>P. aeruginosa<\/jats:italic>\n                    <\/jats:italic>\n                    , causes PG precursors accumulation and significantly reduces AmpC production and beta-lactam resistance in an\n                    <jats:italic>\n                      <jats:italic>ampD<\/jats:italic>\n                    <\/jats:italic>\n                    mutant. These findings highlight the influence of PG precursor dynamics on beta-lactamase regulation and identify DedA4 as a promising therapeutic target. Inhibiting UndP recycling offers a novel strategy to counteract beta-lactam resistance in\n                    <jats:italic>\n                      <jats:italic>P. aeruginosa<\/jats:italic>\n                    <\/jats:italic>\n                    and potentially other AmpC-producing pathogens.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1013633","type":"journal-article","created":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T17:40:57Z","timestamp":1761068457000},"page":"e1013633","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":4,"title":["Disruption of undecaprenyl phosphate recycling suppresses ampC beta-lactamase induction in Pseudomonas aeruginosa"],"prefix":"10.1371","volume":"21","author":[{"given":"Karina","family":"Klycheva","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jo\u00ebl","family":"Gyger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M\u00e9lissa","family":"Frund","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gabriel","family":"Torrens","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Felipe","family":"Cava","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6969-3111","authenticated-orcid":true,"given":"Coralie","family":"Fumeaux","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2025,10,21]]},"reference":[{"key":"ppat.1013633.ref001","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1099\/jmm.0.009142-0","article-title":"Pseudomonas 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