{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,16]],"date-time":"2026-07-16T14:51:37Z","timestamp":1784213497691,"version":"3.55.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1013209","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2025,6,30]],"date-time":"2025-06-30T00:00:00Z","timestamp":1751241600000}}],"reference-count":78,"publisher":"Public Library of Science (PLoS)","issue":"6","license":[{"start":{"date-parts":[[2025,6,16]],"date-time":"2025-06-16T00:00:00Z","timestamp":1750032000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100015691","name":"Division of Microbiology and Infectious Diseases, National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["NIH R01 AI101171"],"award-info":[{"award-number":["NIH R01 AI101171"]}],"id":[{"id":"10.13039\/100015691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35 GM118157"],"award-info":[{"award-number":["R35 GM118157"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000050","name":"National Heart, Lung, and Blood Institute","doi-asserted-by":"publisher","award":["T32 HL094296"],"award-info":[{"award-number":["T32 HL094296"]}],"id":[{"id":"10.13039\/100000050","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100015691","name":"Division of Microbiology and Infectious Diseases, National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["NIH F31AI169971"],"award-info":[{"award-number":["NIH F31AI169971"]}],"id":[{"id":"10.13039\/100015691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000066","name":"National Institute of Environmental Health Sciences","doi-asserted-by":"publisher","award":["NIH T32 ES007028"],"award-info":[{"award-number":["NIH T32 ES007028"]}],"id":[{"id":"10.13039\/100000066","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>To colonize and survive in the host, bacterial pathogens like <jats:italic>Acinetobacter baumannii<\/jats:italic> must acquire zinc (Zn). To maintain Zn homeostasis, <jats:italic>A. baumannii<\/jats:italic> synthesizes proteins of the COG0523 family which are predicted to chaperone Zn to metalloproteins. Bioinformatic tools identified <jats:italic>A. baumannii<\/jats:italic> A1S_0934 as a COG0523 protein, and yeast two-hybrid screening revealed that MurD, an essential muramyl ligase, interacts with A1S_0934. As such, we have named A1S_0934 MurD interacting GTPase COG0523 (MigC). Here we show that MigC is a GTPase whose activity is stimulated upon Zn coordination to a characteristic CxCC (C\u2009=\u2009Cys; x\u2009=\u2009Leu\/Ile\/Met) motif to form a S<jats:sub>3<\/jats:sub>(N\/O) complex. MigC-deficient strains (\u0394<jats:italic>migC<\/jats:italic>) display sensitivity to Zn depletion and exhibit altered cell wall architecture <jats:italic>in vitro<\/jats:italic>. Biochemical and functional assays confirm the MigC-MurD interaction, which inhibits the catalytic activity of MurD. CRISPRi knockdowns of <jats:italic>murD<\/jats:italic> reduce <jats:italic>A. baumannii<\/jats:italic> fitness and increase filamentation during Zn depletion, a phenotype reversed in \u0394<jats:italic>migC<\/jats:italic> strains, suggesting that MigC also inhibits MurD activity in cells. \u0394<jats:italic>migC<\/jats:italic> cells are elongated and sensitized to ceftriaxone, a cephalosporin antibiotic, consistent with decreased cell wall integrity. The \u0394<jats:italic>migC<\/jats:italic> strain has reduced ability to colonize in a murine model of pneumonia highlighting the importance of the MigC-MurD interaction induced by <jats:italic>A. baumannii<\/jats:italic> infection. Together these data suggest that MigC impacts cell wall biogenesis, in part through interactions with MurD, emphasizing the importance of MigC and MurD to the survival and pathogenicity of <jats:italic>A. baumannii<\/jats:italic> while expanding the potential functions of the COG0523 family of enzymes.<\/jats:p>","DOI":"10.1371\/journal.ppat.1013209","type":"journal-article","created":{"date-parts":[[2025,6,16]],"date-time":"2025-06-16T17:43:22Z","timestamp":1750095802000},"page":"e1013209","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":7,"title":["The zinc metalloprotein MigC impacts cell wall biogenesis through interactions with an essential Mur ligase in Acinetobacter baumannii"],"prefix":"10.1371","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3629-8323","authenticated-orcid":true,"given":"Jeanette 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