{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T14:12:27Z","timestamp":1785420747826,"version":"3.56.0"},"reference-count":27,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100003399","name":"Shanghai Municipal Science and Technology Commission","doi-asserted-by":"publisher","award":["22410710300"],"award-info":[{"award-number":["22410710300"]}],"id":[{"id":"10.13039\/501100003399","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81991531"],"award-info":[{"award-number":["81991531"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2026,4,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title\/>\n                    <jats:p>\n                      Two carbapenem-resistant\n                      <jats:italic toggle=\"yes\">Pseudomonas aeruginosa<\/jats:italic>\n                      (CRPA) isolates were collected, which lacked known carbapenemases but produced a \u03b2-lactamase CAE-1. CAE-1 was recently found in\n                      <jats:italic toggle=\"yes\">Comamonas aquatica<\/jats:italic>\n                      and conferred resistance to penicillins and cephalosporins. In this study, we aim to know whether CAE-1 was responsible for the carbapenem resistance in the CRPA isolates and its enzyme hydrolyzing characteristics. Both CRPA clinical isolates exhibited minimal inhibitory concentrations (MICs) of 8 \u00b5g\/mL for imipenem and meropenem, with a positive result in the modified Hodge test for meropenem. The\n                      <jats:italic toggle=\"yes\">bla<\/jats:italic>\n                      <jats:sub>CAE-1<\/jats:sub>\n                      and\n                      <jats:italic toggle=\"yes\">bla<\/jats:italic>\n                      <jats:sub>KPC-2<\/jats:sub>\n                      were cloned and expressed in\n                      <jats:italic toggle=\"yes\">P. aeruginosa<\/jats:italic>\n                      PAO1 and\n                      <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                      DH5\u03b1, respectively. The\n                      <jats:italic toggle=\"yes\">bla<\/jats:italic>\n                      <jats:sub>CAE-1<\/jats:sub>\n                      -carrying PAO1 transformant also tested positive using the modified carbapenem inactivation method and was resistant to piperacillin-tazobactam, ticarcillin-clavulanate, and cefoperazone-sulbactam, but susceptible to ceftazidime-avibactam. Expression of\n                      <jats:italic toggle=\"yes\">bla<\/jats:italic>\n                      <jats:sub>CAE-1<\/jats:sub>\n                      in\n                      <jats:italic toggle=\"yes\">P. aeruginosa<\/jats:italic>\n                      PAO1 elicited a 64- to 128-fold increase in MICs for piperacillin, ceftazidime, cefepime, and aztreonam, and an eightfold increase for meropenem, exhibiting a broader resistance profile than in\n                      <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                      DH5\u03b1. Steady-state kinetic assays showed that CAE-1 had catalytic efficiency against all \u03b2-lactams tested, with comparatively lower efficiency against three carbapenems relative to KPC-2, while demonstrating approximately equivalent efficiency for the other \u03b2-lactam antibiotics tested. Whole-genome sequencing revealed that\n                      <jats:italic toggle=\"yes\">bla<\/jats:italic>\n                      <jats:sub>CAE-1<\/jats:sub>\n                      was a class A \u03b2-lactamase and encoded on an integrative and conjugative element, which might facilitate its horizontal transfer. The class A \u03b2-lactamase CAE-1 is a carbapenemase posing a high risk for horizontal dissemination. Enhanced surveillance for\n                      <jats:italic toggle=\"yes\">bla<\/jats:italic>\n                      <jats:sub>CAE-1<\/jats:sub>\n                      -harboring isolates is needed.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/aac.01362-25","type":"journal-article","created":{"date-parts":[[2026,2,23]],"date-time":"2026-02-23T14:00:16Z","timestamp":1771855216000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":1,"title":["Functional characterization of a novel class A carbapenemase CAE-1 in carbapenem-resistant\n                    <i>Pseudomonas aeruginosa<\/i>\n                    clinical isolates"],"prefix":"10.1128","volume":"70","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-2306-7213","authenticated-orcid":false,"given":"Jinhong","family":"Chen","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/013q1eq08","id-type":"ROR","asserted-by":"publisher"}],"name":"Shanghai Institute of Infectious Disease and Biosecurity, Fudan University","place":["Shanghai, China"]},{"id":[{"id":"https:\/\/ror.org\/013q1eq08","id-type":"ROR","asserted-by":"publisher"}],"name":"Institute of Antibiotics, Huashan Hospital, Fudan University","place":["Shanghai, China"]},{"id":[{"id":"https:\/\/ror.org\/013q1eq08","id-type":"ROR","asserted-by":"publisher"}],"name":"Key Laboratory of Clinical Pharmacology of Antibiotics, National Health Commission of the People's Republic of China","place":["Shanghai, 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