{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T23:01:27Z","timestamp":1791414087489,"version":"4.3.3"},"reference-count":71,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2013,6,1]],"date-time":"2013-06-01T00:00:00Z","timestamp":1370044800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2013,6]]},"abstract":"ABSTRACT<\/jats:title>\n \n Bartonella quintana<\/jats:named-content>\n is a vector-borne bacterial pathogen that causes fatal disease in humans. During the infectious cycle,\n B. quintana<\/jats:named-content>\n transitions from the hemin-restricted human bloodstream to the hemin-rich body louse vector. Because extracytoplasmic function (ECF) sigma factors often regulate adaptation to environmental changes, we hypothesized that a previously unstudied\n B. quintana<\/jats:named-content>\n ECF sigma factor, RpoE, is involved in the transition from the human host to the body louse vector. The genomic context of\n B. quintana<\/jats:named-content>\n rpoE<\/jats:italic>\n identified it as a member of the ECF15 family of sigma factors found only in alphaproteobacteria. ECF15 sigma factors are believed to be the master regulators of the general stress response in alphaproteobacteria. In this study, we examined the\n B. quintana<\/jats:named-content>\n RpoE response to two stressors that are encountered in the body louse vector environment, a decreased temperature and an increased hemin concentration. We determined that the expression of\n rpoE<\/jats:italic>\n is significantly upregulated at the body louse (28\u00b0C) versus the human host (37\u00b0C) temperature.\n rpoE<\/jats:italic>\n expression also was upregulated when\n B. quintana<\/jats:named-content>\n was exposed to high hemin concentrations.\n In vitro<\/jats:italic>\n and\n in vivo<\/jats:italic>\n analyses demonstrated that RpoE function is regulated by a mechanism involving the anti-sigma factor NepR and the response regulator PhyR. The \u0394\n rpoE<\/jats:italic>\n \u0394\n nepR<\/jats:italic>\n mutant strain of\n B. quintana<\/jats:named-content>\n established that RpoE-mediated transcription is important in mediating the tolerance of\n B. quintana<\/jats:named-content>\n to high hemin concentrations. We present the first analysis of an ECF15 sigma factor in a vector-borne human pathogen and conclude that RpoE has a role in the adaptation of\n B. quintana<\/jats:named-content>\n to the hemin-rich arthropod vector environment.\n <\/jats:p>","DOI":"10.1128\/jb.01972-12","type":"journal-article","created":{"date-parts":[[2013,4,6]],"date-time":"2013-04-06T04:37:25Z","timestamp":1365223045000},"page":"2662-2674","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":25,"title":["The Bartonella quintana Extracytoplasmic Function Sigma Factor RpoE Has a Role in Bacterial Adaptation to the Arthropod Vector Environment"],"prefix":"10.1128","volume":"195","author":[{"given":"Stephanie","family":"Abromaitis","sequence":"first","affiliation":[{"name":"Microbial Pathogenesis and Host Defense Program and Division of Infectious Diseases, Department of Medicine, University of California at San Francisco, San Francisco, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jane E.","family":"Koehler","sequence":"additional","affiliation":[{"name":"Microbial Pathogenesis and Host Defense Program and Division of Infectious Diseases, Department of Medicine, University of California at San Francisco, San Francisco, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"crossref","first-page":"713","DOI":"10.4269\/ajtmh.1969.18.713","article-title":"Trench fever. 3. 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