{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:42:37Z","timestamp":1791852157600,"version":"4.3.4"},"reference-count":52,"publisher":"American Society for Microbiology","license":[{"start":{"date-parts":[[2024,4,17]],"date-time":"2024-04-17T00:00:00Z","timestamp":1713312000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/doi.org\/10.1128\/ASMCopyrightv2"},{"start":{"date-parts":[[2024,4,17]],"date-time":"2024-04-17T00:00:00Z","timestamp":1713312000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"crossref","award":["R35GM136213"],"award-info":[{"award-number":["R35GM136213"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"crossref","award":["R35GM141710"],"award-info":[{"award-number":["R35GM141710"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:sec>\n            <jats:title\/>\n            <jats:p>\n              The ribosome is the central hub for protein synthesis and the target of many antibiotics. Although the majority of ribosome-targeting antibiotics inhibit protein synthesis and are bacteriostatic, aminoglycosides promote protein mistranslation and are bactericidal. Understanding the resistance mechanisms of bacteria against aminoglycosides is not only vital for improving the efficacy of this critically important group of antibiotics but also crucial for studying the molecular basis of translational fidelity. In this work, we analyzed\n              <jats:italic>Salmonella<\/jats:italic>\n              mutants evolved in the presence of the aminoglycoside streptomycin (Str) and identified a novel gene\n              <jats:italic>rimP<\/jats:italic>\n              to be involved in Str resistance. RimP is a ribosome assembly factor critical for the maturation of the 30S small subunit that binds Str. Deficiency in RimP increases resistance against Str and facilitates the development of even higher resistance. Deleting\n              <jats:italic>rimP<\/jats:italic>\n              decreases mistranslation and cellular uptake of Str and further impairs flagellar motility. Our work thus highlights a previously unknown mechanism of aminoglycoside resistance via defective ribosome assembly.\n            <\/jats:p>\n          <\/jats:sec>","DOI":"10.1128\/aac.00002-24","type":"journal-article","created":{"date-parts":[[2024,4,17]],"date-time":"2024-04-17T13:01:56Z","timestamp":1713358916000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":3,"title":["Inactivation of the ribosome assembly factor RimP causes streptomycin resistance and impairs motility in\n            <i>Salmonella<\/i>"],"prefix":"10.1128","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-8781-5983","authenticated-orcid":false,"given":"Zhihui","family":"Lyu","sequence":"first","affiliation":[{"name":"Department of Cell Biology and Molecular Genetics, The University of Maryland, College Park, Maryland, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yunyi","family":"Ling","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Molecular Genetics, The University of Maryland, College Park, Maryland, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7800-9764","authenticated-orcid":false,"given":"Ambro","family":"van Hoof","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Molecular Genetics, The University of Texas Health Science Center at Houston, Houston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4466-8304","authenticated-orcid":false,"given":"Jiqiang","family":"Ling","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Molecular Genetics, The University of Maryland, College Park, Maryland, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","published-online":{"date-parts":[[2024,4,17]]},"reference":[{"key":"e_1_3_4_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(21)02724-0"},{"key":"e_1_3_4_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/acsinfecdis.9b00441"},{"key":"e_1_3_4_4_2","volume-title":"Critically important antimicrobials for human medicine","author":"Anonymous","year":"2018","unstructured":"Anonymous. 2018. 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