{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T12:44:11Z","timestamp":1793105051114,"version":"4.5.0"},"reference-count":40,"publisher":"National Academy of Sciences","issue":"19","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2003,9,16]]},"abstract":"\n Borrelia burgdorferi<\/jats:italic>\n (\n Bb<\/jats:italic>\n ), the agent of Lyme disease, exists in nature through a complex enzootic life cycle that involves both ticks and mammals. As\n Bb<\/jats:italic>\n transitions between its two diverse niches, profound adaptive changes occur that are reflected in differential patterns of gene expression, particularly involving lipoprotein genes. Using a mutagenesis approach, we show that Rrp2 (gene BB0763), one of the proteins predicted by the\n Bb<\/jats:italic>\n genome (\n www.tigr.org<\/jats:ext-link>\n ) to be a response regulator of a two-component sensory transduction system, is a pivotal regulator governing the expression of major membrane lipoproteins such as OspC, DbpA, and Mlp8, as well as many other mammalian infection-associated immunogens of\n Bb.<\/jats:italic>\n Sequence analysis additionally suggested that Rrp2 is a bacterial enhancer-binding protein, essential for \u03c3\n 54<\/jats:sup>\n -dependent gene activation. Mutagenesis of a key amino acid residue within a putative activation domain revealed that Rrp2 controlled lipoprotein expression by governing the expression of the alternative \u03c3-factor \u03c3\n s<\/jats:sup>\n in a \u03c3\n 54<\/jats:sup>\n -dependent manner. We therefore propose a signal transduction pathway involving Rrp2, \u03c3\n 54<\/jats:sup>\n , and \u03c3\n s<\/jats:sup>\n , which in concert control the expression of key lipoproteins and other infection-associated immunogens in\n Bb<\/jats:italic>\n .\n <\/jats:p>","DOI":"10.1073\/pnas.1834315100","type":"journal-article","created":{"date-parts":[[2003,9,16]],"date-time":"2003-09-16T13:42:33Z","timestamp":1063719753000},"page":"11001-11006","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":171,"title":["The response regulator Rrp2 is essential for the expression of major membrane lipoproteins in\n Borrelia burgdorferi<\/i>"],"prefix":"10.1073","volume":"100","author":[{"given":"Xiaofeng F.","family":"Yang","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, TX 75390"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sophie M.","family":"Alani","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, TX 75390"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael V.","family":"Norgard","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, TX 75390"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2003,8,29]]},"reference":[{"key":"e_1_3_2_1_2","doi-asserted-by":"publisher","DOI":"10.1080\/21548331.1993.11442776"},{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.7.2909"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.183.1.261"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.183.1.271"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.98.2.670"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/JCM.38.1.382-388.2000"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1038\/37551"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.2000.tb09074.x"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1369-5274(99)80026-5"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.231442498"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.68.1.411-414.2000"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.63.9.3467-3472.1995"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1998.01103.x"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.37.26272"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.67.11.6008-6018.1999"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2000.02104.x"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.71.9.5012-5020.2003"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.70.6.3300-3303.2002"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.68.8.4759-4764.2000"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.65.4.1165-1171.1997"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.67.7.3181-3187.1999"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.69.1.183"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1128\/jcm.30.3.698-703.1992"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2002.02758.x"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1128\/jcm.31.5.1251-1255.1993"},{"key":"e_1_3_2_26_2","unstructured":"Samuels D. 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