{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T17:47:30Z","timestamp":1788371250291,"version":"build-2803163510"},"update-to":[{"DOI":"10.1371\/journal.ppat.1012675","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2024,11,12]],"date-time":"2024-11-12T00:00:00Z","timestamp":1731369600000}}],"reference-count":68,"publisher":"Public Library of Science (PLoS)","issue":"10","license":[{"start":{"date-parts":[[2024,10,31]],"date-time":"2024-10-31T00:00:00Z","timestamp":1730332800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100005088","name":"Beijing Municipal Health Commission","doi-asserted-by":"publisher","award":["Disciplinary Backbone 02-48"],"award-info":[{"award-number":["Disciplinary Backbone 02-48"]}],"id":[{"id":"10.13039\/501100005088","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006668","name":"Oregon Health and Science University","doi-asserted-by":"publisher","award":["Weight Endowed Professorship"],"award-info":[{"award-number":["Weight Endowed Professorship"]}],"id":[{"id":"10.13039\/100006668","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["82330071"],"award-info":[{"award-number":["82330071"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p><jats:italic>Klebsiella pneumoniae<\/jats:italic>, an emerging multidrug-resistant pathogen, exhibits hypermucoviscosity (HMV) as a critical virulence trait mediated by its capsular polysaccharide (CPS). Recent discoveries have determined acetylation as a significant modification for CPS, although its impact on HMV and virulence was previously unknown. This study elucidates the roles of two enzymes: <jats:bold><jats:italic>K<\/jats:italic><\/jats:bold><jats:italic>lebsiella<\/jats:italic> <jats:bold><jats:italic>p<\/jats:italic><\/jats:bold><jats:italic>neumoniae<\/jats:italic> <jats:bold>A<\/jats:bold>cetylated <jats:bold>C<\/jats:bold>PS <jats:bold>E<\/jats:bold>sterase (KpACE), an esterase that removes acetyl groups from CPS, and WcsU, an acetyltransferase that adds acetyl groups to CPS. KpACE is highly upregulated in an <jats:italic>ompR<\/jats:italic>-deficient mutant lacking HMV, and its overexpression consistently reduces HMV and diminishes virulence in a mouse model of pneumonia. The esterase domain-containing KpACE effectively deacetylates model sugar substrates and CPS-K2. Site-directed mutagenesis of the conserved catalytic histidine residue at position 370 significantly reduces its enzymatic activity. This reduction correlates with decreased HMV, affecting key virulence traits including biofilm formation and serum resistance. Similarly, a deficiency in the <jats:italic>wcsU<\/jats:italic> gene abolishes CPS acetylation, and reduces HMV and virulence. These results highlight the importance of the delicate balance between CPS acetylation by WcsU and deacetylation by KpACE in regulating the pathogenicity of <jats:italic>K<\/jats:italic>. <jats:italic>pneumoniae<\/jats:italic>. Understanding this balance provides new insights into the modulation of virulence traits and potential therapeutic targets for combating <jats:italic>K<\/jats:italic>. <jats:italic>pneumoniae<\/jats:italic> infections.<\/jats:p>","DOI":"10.1371\/journal.ppat.1012675","type":"journal-article","created":{"date-parts":[[2024,10,31]],"date-time":"2024-10-31T17:51:08Z","timestamp":1730397068000},"page":"e1012675","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":9,"title":["A novel esterase regulates Klebsiella pneumoniae hypermucoviscosity and 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