{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T01:47:09Z","timestamp":1791942429855,"version":"4.3.4"},"reference-count":39,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2018,6,1]],"date-time":"2018-06-01T00:00:00Z","timestamp":1527811200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31470242"],"award-info":[{"award-number":["31470242"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002855","name":"Ministry of Science and Technology of the People's Republic of China","doi-asserted-by":"publisher","award":["2017YFC1200800"],"award-info":[{"award-number":["2017YFC1200800"]}],"id":[{"id":"10.13039\/501100002855","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2018,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Recent studies revealed that acetylation is a widely used protein modification in prokaryotic organisms. The major protein acetylation acetyltransferase YfiQ and the sirtuin-like deacetylase CobB have been found to be involved in basic physiological processes, such as primary metabolism, chemotaxis, and stress responses, in\n            <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n            and\n            <jats:named-content content-type=\"genus-species\">Salmonella<\/jats:named-content>\n            . However, little is known about protein acetylation modifications in\n            <jats:named-content content-type=\"genus-species\">Yersinia pestis<\/jats:named-content>\n            , a lethal pathogen responsible for millions of human deaths in three worldwide pandemics. Here we found that\n            <jats:italic>Yp_0659<\/jats:italic>\n            and\n            <jats:italic>Yp_1760<\/jats:italic>\n            of\n            <jats:named-content content-type=\"genus-species\">Y. pestis<\/jats:named-content>\n            encode the major protein acetylation acetyltransferase YfiQ and the sirtuin-like deacetylase CobB, respectively, which can acetylate and deacetylate PhoP enzymatically\n            <jats:italic>in vitro<\/jats:italic>\n            . Protein acetylation impairment in\n            <jats:italic>cobB<\/jats:italic>\n            and\n            <jats:italic>yfiQ<\/jats:italic>\n            mutants greatly decreased bacterial tolerance to cold, hot, high-salt, and acidic environments. Our comparative transcriptomic data revealed that the strongly decreased tolerance to stress stimuli was probably related to downregulation of the genes encoding the heat shock proteins (HtpG, HslV, HslR, and IbpA), cold shock proteins (CspC and CspA1), and acid resistance proteins (HdeB and AdiA). We found that the reversible acetylation mediated by CobB and YfiQ conferred attenuation of virulence, probably partially due to the decreased expression of the\n            <jats:italic>psaABCDEF<\/jats:italic>\n            operon, which encodes Psa fimbriae that play a key role in virulence of\n            <jats:named-content content-type=\"genus-species\">Y. pestis<\/jats:named-content>\n            . This is the first report, to our knowledge, on the roles of protein acetylation modification in stress responses, biofilm formation, and virulence of\n            <jats:named-content content-type=\"genus-species\">Y. pestis<\/jats:named-content>\n            .\n          <\/jats:p>","DOI":"10.1128\/iai.00224-18","type":"journal-article","created":{"date-parts":[[2018,4,3]],"date-time":"2018-04-03T12:51:17Z","timestamp":1522759877000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":33,"title":["Protein Acetylation Mediated by YfiQ and CobB Is Involved in the Virulence and Stress Response of Yersinia pestis"],"prefix":"10.1128","volume":"86","author":[{"given":"Wanbing","family":"Liu","sequence":"first","affiliation":[{"name":"State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing, 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Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaoyan","family":"Yang","sequence":"additional","affiliation":[{"name":"Key Laboratory for Plague Prevention and Control of Qinghai Province 2017-ZJ-Y15, Institute for Endemic Disease Prevention and Control of Qinghai Province, Xining, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tong","family":"Wang","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yazhou","family":"Zhou","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing, 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