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However, the mechanism involved remains unknown. In this report, a\n            <jats:italic>\n              csrA\n              <jats:sub>Bb<\/jats:sub>\n            <\/jats:italic>\n            mutant was constructed and complemented in an infectious B31A3 strain. Subsequent animal studies showed that the mutant failed to establish an infection in mice, highlighting that CsrA\n            <jats:sub>Bb<\/jats:sub>\n            is required for the infectivity of\n            <jats:italic>B. burgdorferi<\/jats:italic>\n            . Western blot analyses revealed that the virulence-associated factors OspC, DbpB, and DbpA were attenuated in the\n            <jats:italic>\n              csrA\n              <jats:sub>Bb<\/jats:sub>\n            <\/jats:italic>\n            mutant. The Rrp2-RpoN-RpoS pathway (\u03c3\n            <jats:sup>54<\/jats:sup>\n            -\u03c3\n            <jats:sup>S<\/jats:sup>\n            sigma factor cascade) is a central regulon that governs the expression of\n            <jats:italic>ospC<\/jats:italic>\n            ,\n            <jats:italic>dbpB<\/jats:italic>\n            , and\n            <jats:italic>dbpA<\/jats:italic>\n            . Further analyses found that the level of RpoS was significantly decreased in the mutant, while the level of Rrp2 remained unchanged. A recent study reported that the overexpression of BB0589, a phosphate acetyl-transferase (Pta) that converts acetyl-phosphate to acetyl-coenzyme A (CoA), led to the inhibition of RpoS and OspC expression, suggesting that acetyl-phosphate is an activator of Rrp2. Along with this report, we found that CsrA\n            <jats:sub>Bb<\/jats:sub>\n            binds to the leader sequence of the\n            <jats:italic>bb0589<\/jats:italic>\n            transcript and that the intracellular level of acetyl-CoA in the\n            <jats:italic>\n              csrA\n              <jats:sub>Bb<\/jats:sub>\n            <\/jats:italic>\n            mutant was significantly increased compared to that of the wild type, suggesting that more acetyl-phosphate was being converted to acetyl-CoA in the mutant. Collectively, these results suggest that CsrA\n            <jats:sub>Bb<\/jats:sub>\n            may influence the infectivity of\n            <jats:italic>B. burgdorferi<\/jats:italic>\n            via regulation of acetate metabolism and subsequent activation of the Rrp2-RpoN-RpoS pathway.\n          <\/jats:p>","DOI":"10.1128\/iai.00871-10","type":"journal-article","created":{"date-parts":[[2010,12,21]],"date-time":"2010-12-21T04:53:02Z","timestamp":1292907182000},"page":"1270-1279","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":60,"title":["Inactivation of\n            <i>bb0184<\/i>\n            , Which Encodes Carbon Storage Regulator A, Represses the Infectivity of\n            <i>Borrelia burgdorferi<\/i>"],"prefix":"10.1128","volume":"79","author":[{"given":"Ching Wooen","family":"Sze","sequence":"first","affiliation":[{"name":"Department of Oral Biology, the State University of New York at Buffalo, Buffalo, New York 14214"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chunhao","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Oral Biology, the State University of New York at Buffalo, Buffalo, New York 14214"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.68.12.6790-6797.2000"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2003.03537.x"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.091208.073514"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.mib.2007.03.007"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2002.02982.x"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.01913-06"},{"key":"e_1_3_2_8_2","first-page":"127","volume":"72","year":"1995","unstructured":"Barthold, S. 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