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The gene encodes a 262-amino-acid phosphotransferase, APH(3\u2032)-IVb, sharing only 39.9% amino acid identity with its closest known homolog, APH(3\u2032)-IVa. Heterologous expression of\n                      <jats:italic toggle=\"yes\">aph(3<\/jats:italic>\n                      \u2032\n                      <jats:italic toggle=\"yes\">)-IVb<\/jats:italic>\n                      in\n                      <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                      and a susceptible\n                      <jats:italic toggle=\"yes\">R. anatipestifer<\/jats:italic>\n                      strain conferred resistance to neomycin, paromomycin, and ribostamycin, a phenotype validated by gene deletion and complementation experiments. Kinetic analysis of the purified APH(3\u2032)-IVb enzyme confirmed phosphotransferase activity against these three aminoglycosides, with catalytic efficiencies (\n                      <jats:italic toggle=\"yes\">k<\/jats:italic>\n                      <jats:sub>cat<\/jats:sub>\n                      \/\n                      <jats:italic toggle=\"yes\">\n                        K\n                        <jats:sub>m<\/jats:sub>\n                      <\/jats:italic>\n                      ) ranging from 10\u2074 to 10\u2075 M\u207b\u00b9\u00b7s\u207b\u00b9. Furthermore, site-directed mutagenesis identified key residues critical for enzymatic function. While the prevalence of\n                      <jats:italic toggle=\"yes\">aph(3<\/jats:italic>\n                      \u2032\n                      <jats:italic toggle=\"yes\">)-IVb<\/jats:italic>\n                      in\n                      <jats:italic toggle=\"yes\">R. anatipestifer<\/jats:italic>\n                      isolates was low (1.6%), analysis of public databases identified 93\n                      <jats:italic toggle=\"yes\">aph(3<\/jats:italic>\n                      \u2032\n                      <jats:italic toggle=\"yes\">)-IVb<\/jats:italic>\n                      -positive sequences, of which 36.6% originated from human pathogens. Genetic environment analysis revealed that\n                      <jats:italic toggle=\"yes\">aph(3<\/jats:italic>\n                      \u2032\n                      <jats:italic toggle=\"yes\">)-IVb<\/jats:italic>\n                      resides within a genomic resistance island flanked by mobile genetic elements, suggesting its horizontal acquisition. The emergence of this novel enzyme, coupled with its association with mobile elements and distribution among human pathogens, underscores a potential pathway for resistance dissemination across veterinary and clinical environments, posing a significant public health concern.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/aac.01631-25","type":"journal-article","created":{"date-parts":[[2026,3,24]],"date-time":"2026-03-24T14:40:20Z","timestamp":1774363220000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["Identification and characteristics of a novel acquired aminoglycoside phosphotransferase, APH(3\u2032)-IVb, from\n                    <i>Riemerella anatipestifer<\/i>"],"prefix":"10.1128","volume":"70","author":[{"ORCID":"https:\/\/orcid.org\/0009-0003-2107-2038","authenticated-orcid":false,"given":"Mingkang","family":"Zhou","sequence":"first","affiliation":[{"name":"Research Center of Avian Diseases, College of Veterinary Medicine, Sichuan Agricultural University","place":["Chengdu, China"]},{"name":"Agricultural Animal Diseases and Veterinary Public Health Key Laboratory of Sichuan Province","place":["Chengdu, China"]},{"id":[{"id":"https:\/\/ror.org\/01mv9t934","id-type":"ROR","asserted-by":"publisher"}],"name":"Key Laboratory of Agricultural Bioinformatics, Ministry of Education, Ministry of Education of the People\u2019s Republic of China","place":["Chengdu, China"]},{"name":"International Joint Research Center for Animal Disease Prevention and Control of Sichuan Province","place":["Chengdu, 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