{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T05:17:59Z","timestamp":1790745479633,"version":"4.1.0"},"reference-count":210,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2025,9,18]],"date-time":"2025-09-18T00:00:00Z","timestamp":1758153600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Institutes of Health","award":["AI152983"],"award-info":[{"award-number":["AI152983"]}]},{"name":"National Institutes of Health","award":["AI181738"],"award-info":[{"award-number":["AI181738"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Microorganisms"],"abstract":"<jats:p>Borrelia burgdorferi, the causative agent of Lyme disease, is the most common vector-borne disease in the United States. Compared with other bacterial pathogens, B. burgdorferi has many unique features. For instance, its highly segmented genome was predicted to encode very few proteins directly dedicated to gene expression regulation. Yet, the spirochete continuously reprograms its transcriptome and proteome to promote survival and pathogenesis as spirochetes traverse the enzootic lifecycle between ticks and mammals. Signal sensing systems, a unique alternative sigma factor cascade, and multi-functional regulators work in concert to coordinate virulence gene expression under different tick and mammal environments. In this review, we have summarized recent advances in gene regulation in B. burgdorferi.<\/jats:p>","DOI":"10.3390\/microorganisms13092183","type":"journal-article","created":{"date-parts":[[2025,9,18]],"date-time":"2025-09-18T14:45:46Z","timestamp":1758206746000},"page":"2183","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Virulence Regulation in Borrelia burgdorferi"],"prefix":"10.3390","volume":"13","author":[{"given":"Sierra","family":"George","sequence":"first","affiliation":[{"name":"Department of Molecular Medicine, University of South Florida, 12901 Bruce B Downs Blvd, MDC 07, Tampa, FL 33612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7427-1856","authenticated-orcid":false,"given":"Zhiming","family":"Ouyang","sequence":"additional","affiliation":[{"name":"Department of Molecular Medicine, University of South Florida, 12901 Bruce B Downs Blvd, MDC 07, Tampa, FL 33612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,9,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1126\/science.7043737","article-title":"Lyme disease\u2014A tick-borne spirochetosis?","volume":"216","author":"Burgdorfer","year":"1982","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1038\/37551","article-title":"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi","volume":"390","author":"Fraser","year":"1997","journal-title":"Nature"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/S0168-6445(03)00036-6","article-title":"Adaptation of Borrelia burgdorferi in the tick and the mammalian host","volume":"27","author":"Anguita","year":"2003","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1038\/s41579-020-0400-5","article-title":"Interactions between Borrelia burgdorferi and ticks","volume":"18","author":"Kurokawa","year":"2020","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"e12816","DOI":"10.1111\/pim.12816","article-title":"Interactions between Borrelia burgdorferi and its hosts across the enzootic cycle","volume":"43","author":"Helble","year":"2021","journal-title":"Parasite Immunol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1146\/annurev.micro.112408.134040","article-title":"Gene regulation in Borrelia burgdorferi","volume":"65","author":"Samuels","year":"2011","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.1111\/mmi.15271","article-title":"Lizards and the enzootic cycle of Borrelia burgdorferi sensu lato","volume":"121","author":"Nowak","year":"2024","journal-title":"Mol. Microbiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1089\/vbz.2006.0548","article-title":"Detection of Borrelia burgdorferi DNA in lizards from southern Maryland","volume":"7","author":"Swanson","year":"2007","journal-title":"Vector-Borne Zoonotic Dis."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1128\/iai.51.2.394-396.1986","article-title":"Involvement of birds in the epidemiology of the Lyme disease agent Borrelia burgdorferi","volume":"51","author":"Anderson","year":"1986","journal-title":"Infect. Immun."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1086\/319347","article-title":"Ticks and tickborne bacterial diseases in humans: An emerging infectious threat","volume":"32","author":"Parola","year":"2001","journal-title":"Clin. Infect. Dis."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"101650","DOI":"10.1016\/j.ttbdis.2021.101650","article-title":"Passerine birds as hosts for Ixodes ticks infected with Borrelia burgdorferi sensu stricto in southeastern Virginia","volume":"12","author":"Cumbie","year":"2021","journal-title":"Ticks Tick-Borne Dis."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1016\/j.ttbdis.2018.04.006","article-title":"The role of Ixodes scapularis, Borrelia burgdorferi and wildlife hosts in Lyme disease prevalence: A quantitative review","volume":"9","author":"Halsey","year":"2018","journal-title":"Ticks Tick-Borne Dis."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1086\/318818","article-title":"Effect of tick removal on transmission of Borrelia burgdorferi and Ehrlichia phagocytophila by Ixodes scapularis nymphs","volume":"183","author":"Piesman","year":"2001","journal-title":"J. Infect. Dis."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1093\/jmedent\/45.4.732","article-title":"Transmission dynamics of Borrelia burgdorferi ss during the key third day of feeding by nymphal Ixodes scapularis (Acari: Ixodidae)","volume":"45","author":"Hojgaard","year":"2008","journal-title":"J. Med. Entomol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2240","DOI":"10.1172\/JCI2325","article-title":"A new animal model for studying Lyme disease spirochetes in a mammalian host-adapted state","volume":"101","author":"Akins","year":"1998","journal-title":"J. Clin. Investig."},{"key":"ref_16","first-page":"223","article-title":"Gene Regulation and Transcriptomics","volume":"42","author":"Samuels","year":"2021","journal-title":"Curr. Issues Mol. Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1007\/82_2017_49","article-title":"Regulation of gene and protein expression in the Lyme disease spirochete","volume":"415","author":"Stevenson","year":"2017","journal-title":"Spirochete Biol. Post Genom. Era"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1046\/j.1365-2958.1997.4711838.x","article-title":"The Borrelia burgdorferi circular plasmid cp26: Conservation of plasmid structure and targeted inactivation of the ospC gene","volume":"25","author":"Tilly","year":"1997","journal-title":"Mol. Microbiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"6124","DOI":"10.1128\/JB.00459-06","article-title":"Comparative genome hybridization reveals substantial variation among clinical isolates of Borrelia burgdorferi sensu stricto with different pathogenic properties","volume":"188","author":"Terekhova","year":"2006","journal-title":"J. Bacteriol."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Casjens, S.R., Gilcrease, E.B., Vujadinovic, M., Mongodin, E.F., Luft, B.J., Schutzer, S.E., Fraser, C.M., and Qiu, W.-G. (2017). Plasmid diversity and phylogenetic consistency in the Lyme disease agent Borrelia burgdorferi. BMC Genom., 18.","DOI":"10.1186\/s12864-017-3553-5"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Casjens, S.R., Mongodin, E.F., Qiu, W.-G., Luft, B.J., Schutzer, S.E., Gilcrease, E.B., Huang, W.M., Vujadinovic, M., Aron, J.K., and Vargas, L.C. (2012). Genome stability of Lyme disease spirochetes: Comparative genomics of Borrelia burgdorferi plasmids. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0033280"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1111\/j.1365-2958.2007.05969.x","article-title":"Genetic basis for retention of a critical virulence plasmid of Borrelia burgdorferi","volume":"66","author":"Jewett","year":"2007","journal-title":"Mol. Microbiol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"3561","DOI":"10.1128\/JB.186.11.3561-3569.2004","article-title":"The essential nature of the ubiquitous 26-kilobase circular replicon of Borrelia burgdorferi","volume":"186","author":"Byram","year":"2004","journal-title":"J. Bacteriol."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Hayes, B.M., Dulebohn, D.P., Sarkar, A., Tilly, K., Bestor, A., Ambroggio, X., and Rosa, P.A. (2014). Regulatory protein BBD18 of the lyme disease spirochete: Essential role during tick acquisition?. mBio, 5, Erratum in: MBio 2014, 5. https:\/\/doi.org\/10.1128\/mBio.01608-14.","DOI":"10.1128\/mBio.01608-14"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Dulebohn, D.P., Hayes, B.M., and Rosa, P.A. (2014). Global repression of host-associated genes of the Lyme disease spirochete through post-transcriptional modulation of the alternative sigma factor RpoS. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0093141"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1773","DOI":"10.1128\/IAI.05984-11","article-title":"Altered murine tissue colonization by Borrelia burgdorferi following targeted deletion of linear plasmid 17-carried genes","volume":"80","author":"Casselli","year":"2012","journal-title":"Infect. Immun."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Crowley, M.A., and Bankhead, T. (2022). Potential regulatory role in mammalian host adaptation for a small intergenic region of lp17 in the Lyme disease spirochete. Front. Cell. Infect. Microbiol., 12.","DOI":"10.3389\/fcimb.2022.892220"},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Casselli, T., Crowley, M.A., Highland, M.A., Tourand, Y., and Bankhead, T. (2019). A small intergenic region of lp17 is required for evasion of adaptive immunity and induction of pathology by the Lyme disease spirochete. Cell. Microbiol., 21.","DOI":"10.1111\/cmi.13029"},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Crowley, M.A., and Bankhead, T. (2020). An lp17-encoded small non-coding RNA with a potential regulatory role in mammalian host adaptation by the Lyme disease spirochete. bioRxiv.","DOI":"10.1101\/2020.11.06.371013"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Wong, J.K., Crowley, M.A., and Bankhead, T. (2022). Deletion of a genetic region of lp17 affects plasmid copy number in Borrelia burgdorferi. Front. Cell. Infect. Microbiol., 12.","DOI":"10.3389\/fcimb.2022.884171"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1084\/jem.20031960","article-title":"Essential role for OspA\/B in the life cycle of the Lyme disease spirochete","volume":"199","author":"Yang","year":"2004","journal-title":"J. Exp. Med."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1172\/JCI9427","article-title":"Attachment of Borrelia burgdorferi within Ixodes scapularis mediated by outer surface protein A","volume":"106","author":"Pal","year":"2000","journal-title":"J. Clin. Investig."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Blevins, J.S., Hagman, K.E., and Norgard, M.V. (2008). Assessment of decorin-binding protein A to the infectivity of Borrelia burgdorferi in the murine models of needle and tick infection. BMC Microbiol., 8.","DOI":"10.1186\/1471-2180-8-82"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1128\/IAI.00897-07","article-title":"Both decorin-binding proteins A and B are critical for the overall virulence of Borrelia burgdorferi","volume":"76","author":"Shi","year":"2008","journal-title":"Infect. Immun."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1128\/IAI.69.1.446-455.2001","article-title":"Decreased infectivity in Borrelia burgdorferi strain B31 is associated with loss of linear plasmid 25 or 28-1","volume":"69","author":"Skare","year":"2001","journal-title":"Infect. Immun."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"5938","DOI":"10.1128\/IAI.72.10.5938-5946.2004","article-title":"Experimental assessment of the roles of linear plasmids lp25 and lp28-1 of Borrelia burgdorferi throughout the infectious cycle","volume":"72","author":"Grimm","year":"2004","journal-title":"Infect. Immun."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1358","DOI":"10.1111\/j.1365-2958.2007.05746.x","article-title":"The critical role of the linear plasmid lp36 in the infectious cycle of Borrelia burgdorferi","volume":"64","author":"Jewett","year":"2007","journal-title":"Mol. Microbiol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"5776","DOI":"10.1128\/JB.187.16.5776-5781.2005","article-title":"Role of Borrelia burgdorferi linear plasmid 25 in infection of Ixodes scapularis ticks","volume":"187","author":"Strother","year":"2005","journal-title":"J. Bacteriol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"e0006123","DOI":"10.1128\/iai.00061-23","article-title":"Endogenous Linear Plasmids lp28-4 and lp25 Are Required for Infectivity and Restriction Protection in the Lyme Disease Spirochete Borrelia mayonii","volume":"91","author":"Casselli","year":"2023","journal-title":"Infect. Immun."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"13865","DOI":"10.1073\/pnas.97.25.13865","article-title":"Correlation between plasmid content and infectivity in Borrelia burgdorferi","volume":"97","author":"Purser","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1089\/vbz.2005.5.237","article-title":"Plasmid requirements for infection of ticks by Borrelia burgdorferi","volume":"5","author":"Strother","year":"2005","journal-title":"Vector-Borne Zoonotic Dis."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"2909","DOI":"10.1073\/pnas.92.7.2909","article-title":"Induction of an outer surface protein on Borrelia burgdorferi during tick feeding","volume":"92","author":"Schwan","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"3181","DOI":"10.1128\/IAI.67.7.3181-3187.1999","article-title":"Effects of environmental pH on membrane proteins in Borrelia burgdorferi","volume":"67","author":"Carroll","year":"1999","journal-title":"Infect. Immun."},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Bontemps-Gallo, S., Lawrence, K., and Gherardini, F.C. (2016). Two different virulence-related regulatory pathways in Borrelia burgdorferi are directly affected by osmotic fluxes in the blood meal of feeding Ixodes ticks. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005791"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1580","DOI":"10.1128\/IAI.72.3.1580-1586.2004","article-title":"Dissolved oxygen levels alter gene expression and antigen profiles in Borrelia burgdorferi","volume":"72","author":"Seshu","year":"2004","journal-title":"Infect. Immun."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"11684","DOI":"10.1073\/pnas.2032956100","article-title":"Borrelia oxidative stress response regulator, BosR: A distinctive Zn-dependent transcriptional activator","volume":"100","author":"Boylan","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"10-1128","DOI":"10.1128\/microbiolspec.MBP-0011-2014","article-title":"Borrelia burgdorferi: Carbon metabolism and the tick-mammal enzootic cycle","volume":"3","author":"Corona","year":"2015","journal-title":"Microbiol. Spectr."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Tiwari, S., Jamal, S.B., Hassan, S.S., Carvalho, P.V., Almeida, S., Barh, D., Ghosh, P., Silva, A., Castro, T.L., and Azevedo, V. (2017). Two-component signal transduction systems of pathogenic bacteria as targets for antimicrobial therapy: An overview. Front. Microbiol., 8.","DOI":"10.3389\/fmicb.2017.01878"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1016\/j.mib.2010.01.008","article-title":"Two-component signal transduction as potential drug targets in pathogenic bacteria","volume":"13","author":"Gotoh","year":"2010","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.mib.2006.01.005","article-title":"Regulation of bacterial virulence by two-component systems","volume":"9","author":"Beier","year":"2006","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1146\/annurev.micro.091208.073214","article-title":"Biological insights from structures of two-component proteins","volume":"63","author":"Gao","year":"2009","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"3752","DOI":"10.1016\/j.jmb.2016.08.003","article-title":"Molecular mechanisms of two-component signal transduction","volume":"428","author":"Zschiedrich","year":"2016","journal-title":"J. Mol. Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1448","DOI":"10.1074\/jbc.M410104200","article-title":"Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli","volume":"280","author":"Yamamoto","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"7145","DOI":"10.1128\/JB.183.24.7365-7370.2001","article-title":"Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems","volume":"183","author":"Kobayashi","year":"2001","journal-title":"J. Bacteriol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1666","DOI":"10.1111\/j.1462-2920.2011.02495.x","article-title":"Key two-component regulatory systems that control biofilm formation in Pseudomonas aeruginosa","volume":"13","author":"Mikkelsen","year":"2011","journal-title":"Environ. Microbiol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"3117","DOI":"10.1128\/IAI.05136-11","article-title":"The hybrid histidine kinase Hk1 is part of a two-component system that is essential for survival of Borrelia burgdorferi in feeding Ixodes scapularis ticks","volume":"79","author":"Caimano","year":"2011","journal-title":"Infect. Immun."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1111\/j.1365-2958.2011.07687.x","article-title":"The diguanylate cyclase, Rrp1, regulates critical steps in the enzootic cycle of the Lyme disease spirochetes","volume":"81","author":"Kostick","year":"2011","journal-title":"Mol. Microbiol."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"He, M., Ouyang, Z., Troxell, B., Xu, H., Moh, A., Piesman, J., Norgard, M.V., Gomelsky, M., and Yang, X.F. (2011). Cyclic di-GMP is essential for the survival of the Lyme disease spirochete in ticks. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002133"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1792","DOI":"10.1128\/JB.187.5.1792-1798.2005","article-title":"Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: Insights into biochemistry of the GGDEF protein domain","volume":"187","author":"Ryjenkov","year":"2005","journal-title":"J. Bacteriol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.1111\/j.1365-2958.2009.06621.x","article-title":"Rrp1, a cyclic-di-GMP-producing response regulator, is an important regulator of Borrelia burgdorferi core cellular functions","volume":"71","author":"Rogers","year":"2009","journal-title":"Mol. Microbiol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1111\/mmi.15254","article-title":"Borrelia burgdorferi PlzA is a cyclic-di-GMP dependent DNA and RNA binding protein","volume":"121","author":"Jusufovic","year":"2024","journal-title":"Mol. Microbiol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1111\/j.1574-695X.2009.00635.x","article-title":"Identification and molecular characterization of a cyclic-di-GMP effector protein, PlzA (BB0733): Additional evidence for the existence of a functional cyclic-di-GMP regulatory network in the Lyme disease spirochete, Borrelia burgdorferi","volume":"58","author":"Freedman","year":"2010","journal-title":"FEMS Immunol. Med. Microbiol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1815","DOI":"10.1128\/IAI.00075-11","article-title":"Analysis of the Borrelia burgdorferi cyclic-di-GMP-binding protein PlzA reveals a role in motility and virulence","volume":"79","author":"Pitzer","year":"2011","journal-title":"Infect. Immun."},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Novak, E.A., Sultan, S.Z., and Motaleb, M.A. (2014). The cyclic-di-GMP signaling pathway in the Lyme disease spirochete, Borrelia burgdorferi. Front. Cell. Infect. Microbiol., 4.","DOI":"10.3389\/fcimb.2014.00056"},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Groshong, A.M., Grassmann, A.A., Luthra, A., McLain, M.A., Provatas, A.A., Radolf, J.D., and Caimano, M.J. (2021). PlzA is a bifunctional c-di-GMP biosensor that promotes tick and mammalian host-adaptation of Borrelia burgdorferi. PLoS Pathog., 17.","DOI":"10.1371\/journal.ppat.1009725"},{"key":"ref_66","doi-asserted-by":"crossref","unstructured":"Zhang, J.-J., Chen, T., Yang, Y., Du, J., Li, H., Troxell, B., He, M., Carrasco, S.E., Gomelsky, M., and Yang, X.F. (2018). Positive and negative regulation of glycerol utilization by the c-di-GMP binding protein PlzA in Borrelia burgdorferi. J. Bacteriol., 200.","DOI":"10.1128\/JB.00243-18"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1128\/IAI.01238-13","article-title":"Cyclic di-GMP receptor PlzA controls virulence gene expression through RpoS in Borrelia burgdorferi","volume":"82","author":"He","year":"2014","journal-title":"Infect. Immun."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1775","DOI":"10.1128\/IAI.00050-13","article-title":"Study of the response regulator Rrp1 reveals its regulatory role in chitobiose utilization and virulence of Borrelia burgdorferi","volume":"81","author":"Sze","year":"2013","journal-title":"Infect. Immun."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"11001","DOI":"10.1073\/pnas.1834315100","article-title":"The response regulator Rrp2 is essential for the expression of major membrane lipoproteins in Borrelia burgdorferi","volume":"100","author":"Yang","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"3844","DOI":"10.1128\/IAI.00467-08","article-title":"Essential role of the response regulator Rrp2 in the infectious cycle of Borrelia burgdorferi","volume":"76","author":"Boardman","year":"2008","journal-title":"Infect. Immun."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Xu, H., Caimano, M.J., Lin, T., He, M., Radolf, J.D., Norris, S.J., Gheradini, F., Wolfe, A.J., and Yang, X.F. (2010). Correction: Role of Acetyl-Phosphate in Activation of the Rrp2-RpoN-RpoS Pathway in Borrelia burgdorferi. PLoS Pathog., 6.","DOI":"10.1371\/annotation\/88293342-3534-4b8b-8800-c63a8c86bf6d"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1111\/j.1365-2958.2007.05813.x","article-title":"Insights into the complex regulation of rpoS in Borrelia burgdorferi","volume":"65","author":"Burtnick","year":"2007","journal-title":"Mol. Microbiol."},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Liu, Q., Xu, H., Zhang, Y., Yang, J., Du, J., Zhou, Y., Yang, X.F., and Lou, Y. (2021). Corrigendum: Role of HK2 in the Enzootic Cycle of Borrelia burgdorferi. Front. Med., 8.","DOI":"10.3389\/fmed.2021.668709"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2641","DOI":"10.1099\/mic.0.2008\/019992-0","article-title":"Transcriptional interplay among the regulators Rrp2, RpoN and RpoS in Borrelia burgdorferi","volume":"154","author":"Ouyang","year":"2008","journal-title":"Microbiology"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Ouyang, Z., Zhou, J., and Norgard, M.V. (2014). Synthesis of RpoS is dependent on a putative enhancer binding protein Rrp2 in Borrelia burgdorferi. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0096917"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"6433","DOI":"10.1128\/IAI.72.11.6433-6445.2004","article-title":"RpoS is not central to the general stress response in Borrelia burgdorferi but does control expression of one or more essential virulence determinants","volume":"72","author":"Caimano","year":"2004","journal-title":"Infect. Immun."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.1111\/j.1365-2958.2007.05860.x","article-title":"Analysis of the RpoS regulon in Borrelia burgdorferi in response to mammalian host signals provides insight into RpoS function during the enzootic cycle","volume":"65","author":"Caimano","year":"2007","journal-title":"Mol. Microbiol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"2902","DOI":"10.1128\/JB.01721-08","article-title":"Rrp2, a \u03c354-dependent transcriptional activator of Borrelia burgdorferi, activates rpoS in an enhancer-independent manner","volume":"191","author":"Blevins","year":"2009","journal-title":"J. Bacteriol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"3336","DOI":"10.1128\/JB.00253-12","article-title":"Rrp2, a prokaryotic enhancer-like binding protein, is essential for viability of Borrelia burgdorferi","volume":"194","author":"Groshong","year":"2012","journal-title":"J. Bacteriol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1128\/JB.01010-15","article-title":"Insight into the dual functions of bacterial enhancer-binding protein Rrp2 of Borrelia burgdorferi","volume":"198","author":"Yin","year":"2016","journal-title":"J. Bacteriol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1111\/mmi.13545","article-title":"The putative Walker A and Walker B motifs of R rp2 are required for the growth of B orrelia burgdorferi","volume":"103","author":"Ouyang","year":"2017","journal-title":"Mol. Microbiol."},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Raghunandanan, S., Zhang, K., Zhang, Y., Priya, R., Sze, C.W., Lou, Y., Lynch, M.J., Crane, B.R., Kaplan, M.H., and Li, C. (2024). MCP5, a methyl-accepting chemotaxis protein regulated by both the Hk1-Rrp1 and Rrp2-RpoN-RpoS pathways, is required for the immune evasion of Borrelia burgdorferi. PLoS Pathog., 20.","DOI":"10.1101\/2024.06.10.598185"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"e166710","DOI":"10.1172\/JCI166710","article-title":"BosR and PlzA reciprocally regulate RpoS function to sustain Borrelia burgdorferi in ticks and mammals","volume":"133","author":"Grassmann","year":"2023","journal-title":"J. Clin. Investig."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1038\/nrmicro787","article-title":"The regulation of bacterial transcription initiation","volume":"2","author":"Browning","year":"2004","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1038\/s41576-020-0254-8","article-title":"Redefining fundamental concepts of transcription initiation in bacteria","volume":"21","author":"Busby","year":"2020","journal-title":"Nat. Rev. Genet."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1146\/annurev-micro-092611-150012","article-title":"Activating transcription in bacteria","volume":"66","author":"Lee","year":"2012","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0959-440X(00)00185-8","article-title":"Bacterial RNA polymerase","volume":"11","author":"Darst","year":"2001","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"848","DOI":"10.3390\/biom5020848","article-title":"Structural biology of bacterial RNA polymerase","volume":"5","author":"Murakami","year":"2015","journal-title":"Biomolecules"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1128\/MMBR.69.4.527-543.2005","article-title":"Alternative sigma factors and their roles in bacterial virulence","volume":"69","author":"Kazmierczak","year":"2005","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Roberts, M., Rowley, G., Kormanec, J., and Zalm, M.E.J. (2017). The role of alternative sigma factors in pathogen virulence. Foodborne Pathogens: Virulence Factors Host Susceptibility, Springer.","DOI":"10.1007\/978-3-319-56836-2_9"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.3390\/biom5031245","article-title":"Bacterial sigma factors and anti-sigma factors: Structure, function and distribution","volume":"5","author":"Paget","year":"2015","journal-title":"Biomolecules"},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Schellhorn, H.E. (2020). Function, evolution, and composition of the RpoS regulon in Escherichia coli. Front. Microbiol., 11.","DOI":"10.3389\/fmicb.2020.560099"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1146\/annurev-micro-090110-102946","article-title":"The RpoS-mediated general stress response in Escherichia coli","volume":"65","author":"Battesti","year":"2011","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1099\/13500872-145-4-835","article-title":"RpoS-dependent stress tolerance in Pseudomonas aeruginosa","volume":"145","author":"Bally","year":"1999","journal-title":"Microbiology"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1111\/j.1574-6976.2007.00092.x","article-title":"Sigma factors in Pseudomonas aeruginosa","volume":"32","author":"Potvin","year":"2008","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Caimano, M.J., Groshong, A.M., Belperron, A., Mao, J., Hawley, K.L., Luthra, A., Graham, D.E., Earnhart, C.G., Marconi, R.T., and Bockenstedt, L.K. (2019). The RpoS Gatekeeper in Borrelia burgdorferi: An Invariant Regulatory Scheme That Promotes Spirochete Persistence in Reservoir Hosts and Niche Diversity. Front. Microbiol., 10.","DOI":"10.3389\/fmicb.2019.01923"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"12724","DOI":"10.1073\/pnas.231442498","article-title":"Expression of Borrelia burgdorferi OspC and DbpA is controlled by a RpoN\u2013RpoS regulatory pathway","volume":"98","author":"Yang","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"4822","DOI":"10.1128\/JB.187.14.4822-4829.2005","article-title":"Analysis of the ospC regulatory element controlled by the RpoN-RpoS regulatory pathway in Borrelia burgdorferi","volume":"187","author":"Yang","year":"2005","journal-title":"J. Bacteriol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"3547","DOI":"10.1128\/IAI.00158-06","article-title":"Delineating the requirement for the Borrelia burgdorferi virulence factor OspC in the mammalian host","volume":"74","author":"Stewart","year":"2006","journal-title":"Infect. Immun."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Ouyang, Z., Narasimhan, S., Neelakanta, G., Kumar, M., Pal, U., Fikrig, E., and Norgard, M.V. (2012). Activation of the RpoN-RpoS regulatory pathway during the enzootic life cycle of Borrelia burgdorferi. BMC Microbiol., 12.","DOI":"10.1186\/1471-2180-12-44"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"2139","DOI":"10.1128\/JB.01653-06","article-title":"Evidence that RpoS (\u03c3S) in Borrelia burgdorferi is controlled directly by RpoN (\u03c354\/\u03c3N)","volume":"189","author":"Smith","year":"2007","journal-title":"J. Bacteriol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S1369-5274(00)00070-9","article-title":"Two-component and phosphorelay signal transduction","volume":"3","author":"Hoch","year":"2000","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.1111\/j.1365-2958.2009.06945.x","article-title":"BosR (BB0647) governs virulence expression in Borrelia burgdorferi","volume":"74","author":"Ouyang","year":"2009","journal-title":"Mol. Microbiol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1344","DOI":"10.1111\/j.1365-2958.2009.06951.x","article-title":"The BosR regulatory protein of Borrelia burgdorferi interfaces with the RpoS regulatory pathway and modulates both the oxidative stress response and pathogenic properties of the Lyme disease spirochete","volume":"74","author":"Hyde","year":"2009","journal-title":"Mol. Microbiol."},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Ouyang, Z., Deka, R.K., and Norgard, M.V. (2011). BosR (BB0647) controls the RpoN-RpoS regulatory pathway and virulence expression in Borrelia burgdorferi by a novel DNA-binding mechanism. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1001272"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"6443","DOI":"10.1128\/JB.186.19.6443-6456.2004","article-title":"The fur homologue in Borrelia burgdorferi","volume":"186","author":"Katona","year":"2004","journal-title":"J. Bacteriol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1126\/science.288.5471.1651","article-title":"Lack of a role for iron in the Lyme disease pathogen","volume":"288","author":"Posey","year":"2000","journal-title":"Science"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1099\/mic.0.075655-0","article-title":"Identification of a core sequence for the binding of BosR to the rpoS promoter region in Borrelia burgdorferi","volume":"160","author":"Ouyang","year":"2014","journal-title":"Microbiology"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"4932","DOI":"10.1128\/JB.183.16.4932-4937.2001","article-title":"Iron-dependent transcription of the frpB gene of Helicobacter pylori is controlled by the Fur repressor protein","volume":"183","author":"Delany","year":"2001","journal-title":"J. Bacteriol."},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Sun, F., Gao, H., Zhang, Y., Wang, L., Fang, N., Tan, Y., Guo, Z., Xia, P., Zhou, D., and Yang, R. (2012). Fur is a repressor of biofilm formation in Yersinia pestis. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0052392"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"32100","DOI":"10.1074\/jbc.M404924200","article-title":"The ferric uptake regulator (Fur) protein from Bradyrhizobium japonicum is an iron-responsive transcriptional repressor in vitro","volume":"279","author":"Friedman","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"2590","DOI":"10.1128\/IAI.00116-09","article-title":"This is not your mother\u2019s repressor: The complex role of fur in pathogenesis","volume":"77","author":"Carpenter","year":"2009","journal-title":"Infect. Immun."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"5320","DOI":"10.1093\/nar\/gkae114","article-title":"A Fur family protein BosR is a novel RNA-binding protein that controls rpoS RNA stability in the Lyme disease pathogen","volume":"52","author":"Raghunandanan","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"2243","DOI":"10.1099\/mic.0.000166","article-title":"The Fur homologue BosR requires Arg39 to activate rpoS transcription in Borrelia burgdorferi and thereby direct spirochaete infection in mice","volume":"161","author":"Katona","year":"2015","journal-title":"Microbiology"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"2599","DOI":"10.1099\/mic.0.28996-0","article-title":"Transcriptional profiling of Borrelia burgdorferi containing a unique bosR allele identifies a putative oxidative stress regulon","volume":"152","author":"Hyde","year":"2006","journal-title":"Microbiology"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"2566","DOI":"10.1128\/IAI.00297-16","article-title":"Evidence that BosR (BB0647) is a positive autoregulator in Borrelia burgdorferi","volume":"84","author":"Ouyang","year":"2016","journal-title":"Infect. Immun."},{"key":"ref_117","doi-asserted-by":"crossref","unstructured":"Raghunandanan, S., Priya, R., Lin, G., Alanazi, F., Zoss, A., Warren, E., Stewart, P., and Yang, X.F. (2025). Positive feedback regulation between RpoS and BosR in the Lyme disease pathogen. mBio, 16.","DOI":"10.1128\/mbio.02766-24"},{"key":"ref_118","doi-asserted-by":"crossref","unstructured":"Mason, C., Liu, X., Prabhudeva, S., and Ouyang, Z. (2019). The CXXC motifs are essential for the function of BosR in Borrelia burgdorferi. Front. Cell. Infect. Microbiol., 9.","DOI":"10.3389\/fcimb.2019.00109"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1111\/mmi.12068","article-title":"A novel iron-and copper-binding protein in the L yme disease spirochaete","volume":"86","author":"Wang","year":"2012","journal-title":"Mol. Microbiol."},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Wang, P., Yu, Z., Santangelo, T.J., Olesik, J., Wang, Y., Heldwein, E., and Li, X. (2017). BosR is a novel fur family member responsive to copper and regulating copper homeostasis in Borrelia burgdorferi. J. Bacteriol., 199.","DOI":"10.1128\/JB.00276-17"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1111\/j.1365-2958.2007.05716.x","article-title":"Temperature-induced regulation of RpoS by a small RNA in Borrelia burgdorferi","volume":"64","author":"Lybecker","year":"2007","journal-title":"Mol. Microbiol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1111\/j.1365-2958.2010.07374.x","article-title":"Identification and function of the RNA chaperone Hfq in the Lyme disease spirochete Borrelia burgdorferi","volume":"78","author":"Lybecker","year":"2010","journal-title":"Mol. Microbiol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"10417","DOI":"10.1038\/s41467-024-54806-w","article-title":"Broadly conserved FlgV controls flagellar assembly and Borrelia burgdorferi dissemination in mice","volume":"15","author":"Soliman","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1128\/IAI.00882-10","article-title":"CsrA modulates levels of lipoproteins and key regulators of gene expression critical for pathogenic mechanisms of Borrelia burgdorferi","volume":"79","author":"Karna","year":"2011","journal-title":"Infect. Immun."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"5149","DOI":"10.1128\/IAI.00673-09","article-title":"Overexpression of CsrA (BB0184) alters the morphology and antigen profiles of Borrelia burgdorferi","volume":"77","author":"Sanjuan","year":"2009","journal-title":"Infect. Immun."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1270","DOI":"10.1128\/IAI.00871-10","article-title":"Inactivation of bb0184, which encodes carbon storage regulator A, represses the infectivity of Borrelia burgdorferi","volume":"79","author":"Sze","year":"2011","journal-title":"Infect. Immun."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"2972","DOI":"10.1128\/IAI.00494-13","article-title":"Contributions of environmental signals and conserved residues to the functions of carbon storage regulator A of Borrelia burgdorferi","volume":"81","author":"Karna","year":"2013","journal-title":"Infect. Immun."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1128\/IAI.01555-13","article-title":"CsrA (BB0184) is not involved in activation of the RpoN-RpoS regulatory pathway in Borrelia burgdorferi","volume":"82","author":"Ouyang","year":"2014","journal-title":"Infect. Immun."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1111\/mmi.12171","article-title":"Borrelia host adaptation Regulator (BadR) regulates rpoS to modulate host adaptation and virulence factors in Borrelia burgdorferi","volume":"88","author":"Miller","year":"2013","journal-title":"Mol. Microbiol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1111\/mmi.13206","article-title":"BadR (BB0693) controls growth phase-dependent induction of rpoS and bosR in Borrelia burgdorferi via recognizing TAAAATAT motifs","volume":"98","author":"Ouyang","year":"2015","journal-title":"Mol. Microbiol."},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"George, S., and Ouyang, Z. (2025). Analysis of the BadR regulon in Borrelia burgdorferi. BMC Microbiol., 25.","DOI":"10.1186\/s12866-025-03797-9"},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Arnold, W.K., Savage, C.R., Lethbridge, K.G., Smith, T.C., Brissette, C.A., Seshu, J., and Stevenson, B. (2018). Transcriptomic insights on the virulence-controlling CsrA, BadR, RpoN, and RpoS regulatory networks in the Lyme disease spirochete. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0203286"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"e0034023","DOI":"10.1128\/jb.00340-23","article-title":"BadR directly represses the expression of the glycerol utilization operon in the Lyme disease pathogen","volume":"206","author":"Zhang","year":"2024","journal-title":"J. Bacteriol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.bbrc.2023.02.044","article-title":"Quantitative analyses of interactions between SpoVG and RNA\/DNA","volume":"654","author":"Saylor","year":"2023","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Savage, C.R., Jutras, B.L., Bestor, A., Tilly, K., Rosa, P.A., Tourand, Y., Stewart, P.E., Brissette, C.A., and Stevenson, B. (2018). Borrelia burgdorferi SpoVG DNA-and RNA-binding protein modulates the physiology of the Lyme disease spirochete. J. Bacteriol., 200.","DOI":"10.1128\/JB.00033-18"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1111\/mmi.14336","article-title":"The Lyme disease spirochete\u2019s BpuR DNA\/RNA-binding protein is differentially expressed during the mammal\u2013tick infectious cycle, which affects translation of the SodA superoxide dismutase","volume":"112","author":"Jutras","year":"2019","journal-title":"Mol. Microbiol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1111\/mmi.15066","article-title":"c-di-GMP regulates activity of the PlzA RNA chaperone from the Lyme disease spirochete","volume":"119","author":"Patel","year":"2023","journal-title":"Mol. Microbiol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1038\/s41467-023-35897-3","article-title":"Coupled induction of prophage and virulence factors during tick transmission of the Lyme disease spirochete","volume":"14","author":"Wachter","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1111\/mmi.14504","article-title":"DksA plays an essential role in regulating the virulence of Borrelia burgdorferi","volume":"114","author":"Mason","year":"2020","journal-title":"Mol. Microbiol."},{"key":"ref_140","doi-asserted-by":"crossref","unstructured":"Boyle, W.K., Richards, C.L., Dulebohn, D.P., Zalud, A.K., Shaw, J.A., Lovas, S., Gherardini, F.C., and Bourret, T.J. (2021). DksA-dependent regulation of RpoS contributes to Borrelia burgdorferi tick-borne transmission and mammalian infectivity. PLoS Pathog., 17.","DOI":"10.1371\/journal.ppat.1009072"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1111\/mmi.14460","article-title":"The Lon-2 protease of Borrelia burgdorferi is critical for infection in the mammalian host","volume":"113","author":"Mason","year":"2020","journal-title":"Mol. Microbiol."},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Thompson, C., Mason, C., Parrilla, S., and Ouyang, Z. (2020). The Lon-1 protease is required by Borrelia burgdorferi to infect the mammalian host. Infect. Immun., 88.","DOI":"10.1128\/IAI.00951-19"},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Burke, T.P., and Portnoy, D.A. (2016). SpoVG is a conserved RNA-binding protein that regulates Listeria monocytogenes lysozyme resistance, virulence, and swarming motility. MBio, 7.","DOI":"10.1128\/mBio.00240-16"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"106144","DOI":"10.1016\/j.micpath.2023.106144","article-title":"The global regulator SpoVG regulates Listeria monocytogenes biofilm formation","volume":"180","author":"Shi","year":"2023","journal-title":"Microb. Pathog."},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Huang, Q., Zhang, Z., Liu, Q., Liu, F., Liu, Y., Zhang, J., and Wang, G. (2021). SpoVG is an important regulator of sporulation and affects biofilm formation by regulating Spo0A transcription in Bacillus cereus 0\u20139. BMC Microbiol., 21.","DOI":"10.1186\/s12866-021-02239-6"},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"Zhu, Q., Liu, B., and Sun, B. (2020). SpoVG modulates cell aggregation in Staphylococcus aureus by regulating sasC expression and extracellular DNA release. Appl. Environ. Microbiol., 86.","DOI":"10.1128\/AEM.00591-20"},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"Sch\u00fcrmann, J., Fischer, M.A., Herzberg, M., Reemtsma, T., Strommenger, B., Werner, G., Schuster, C.F., and Layer-Nicolaou, F. (2024). The genes mgtE and spoVG are involved in zinc tolerance of Staphylococcus aureus. Appl. Environ. Microbiol., 90.","DOI":"10.1128\/aem.00453-24"},{"key":"ref_148","doi-asserted-by":"crossref","unstructured":"Jutras, B.L., Chenail, A.M., Rowland, C.L., Carroll, D., Miller, M.C., Bykowski, T., and Stevenson, B. (2013). Eubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0066683"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"26220","DOI":"10.1074\/jbc.M113.491357","article-title":"Bpur, the Lyme disease spirochete\u2019s PUR domain protein: Identification as a transcriptional modulator and characterization of nucleic acid interactions","volume":"288","author":"Jutras","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Graebsch, A., Roche, S., Kostrewa, D., S\u00f6ding, J., and Niessing, D. (2010). Of bits and bugs\u2014On the use of bioinformatics and a bacterial crystal structure to solve a eukaryotic repeat-protein structure. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0013402"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"4915","DOI":"10.1128\/JB.00819-13","article-title":"Posttranscriptional self-regulation by the Lyme disease bacterium\u2019s BpuR DNA\/RNA-binding protein","volume":"195","author":"Jutras","year":"2013","journal-title":"J. Bacteriol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1111\/j.1365-2958.2008.06549.x","article-title":"sodA is essential for virulence of Borrelia burgdorferi in the murine model of Lyme disease","volume":"71","author":"Elliott","year":"2009","journal-title":"Mol. Microbiol."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Esteve-Gassent, M.D., Smith, T.C., Small, C.M., Thomas, D.P., and Seshu, J. (2015). Absence of sodA increases the levels of oxidation of key metabolic determinants of Borrelia burgdorferi. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0136707"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1046\/j.1365-2958.2002.02758.x","article-title":"Identification of loci critical for replication and compatibility of a Borrelia burgdorferi cp32 plasmid and use of a cp32-based shuttle vector for the expression of fluorescent reporters in the Lyme disease spirochaete","volume":"43","author":"Eggers","year":"2002","journal-title":"Mol. Microbiol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1046\/j.1365-2958.2001.02256.x","article-title":"Isolation of a circular plasmid region sufficient for autonomous replication and transformation of infectious Borrelia burgdorferi","volume":"39","author":"Stewart","year":"2001","journal-title":"Mol. Microbiol."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"3202","DOI":"10.1128\/JB.185.10.3202-3209.2003","article-title":"Conservation of plasmid maintenance functions between linear and circular plasmids in Borrelia burgdorferi","volume":"185","author":"Stewart","year":"2003","journal-title":"J. Bacteriol."},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Chenail, A.M., Jutras, B.L., Adams, C.A., Burns, L.H., Bowman, A., Verma, A., and Stevenson, B. (2017). Correction for Chenail et al., \u201cBorrelia burgdorferi cp32 BpaB modulates expression of the prophage NucP nuclease and SsbP single-stranded DNA-binding protein\u201d. J. Bacteriol., 199.","DOI":"10.1128\/JB.00400-17"},{"key":"ref_158","doi-asserted-by":"crossref","unstructured":"Cooley, A.E., Riley, S.P., Kral, K., Miller, M.C., DeMoll, E., Fried, M.G., and Stevenson, B. (2009). DNA-binding by Haemophilus influenzae and Escherichia coli YbaB, members of a widely-distributed bacterial protein family. BMC Microbiol., 9.","DOI":"10.1186\/1471-2180-9-137"},{"key":"ref_159","doi-asserted-by":"crossref","unstructured":"Pal, P., Modi, M., Ravichandran, S., Yennamalli, R.M., and Priyadarshini, R. (2021). DNA-binding properties of YbaB, a putative nucleoid-associated protein from Caulobacter crescentus. Front. Microbiol., 12.","DOI":"10.3389\/fmicb.2021.733344"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"1973","DOI":"10.1093\/nar\/gkp027","article-title":"Borrelia burgdorferi EbfC defines a newly-identified, widespread family of bacterial DNA-binding proteins","volume":"37","author":"Riley","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"ref_161","doi-asserted-by":"crossref","unstructured":"Cordeiro, T.F.V.B., Gontijo, M.T.P., Jorge, G.P., and Brocchi, M. (2022). EbfC\/YbaB: A widely distributed nucleoid-associated protein in prokaryotes. Microorganisms, 10.","DOI":"10.3390\/microorganisms10101945"},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1002\/prot.10297","article-title":"Crystal structure of YbaB from Haemophilus influenzae (HI0442), a protein of unknown function coexpressed with the recombinational DNA repair protein RecR","volume":"50","author":"Lim","year":"2003","journal-title":"Proteins Struct. Funct. Bioinform."},{"key":"ref_163","doi-asserted-by":"crossref","unstructured":"Krusenstjerna, A.C., Saylor, T.C., Arnold, W.K., Tucker, J.S., and Stevenson, B. (2023). Borrelia burgdorferi DnaA and the nucleoid-associated protein EbfC coordinate expression of the dnaX-ebfC operon. J. Bacteriol., 205.","DOI":"10.1128\/jb.00396-22"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"3395","DOI":"10.1128\/JB.00252-12","article-title":"EbfC (YbaB) is a new type of bacterial nucleoid-associated protein and a global regulator of gene expression in the Lyme disease spirochete","volume":"194","author":"Jutras","year":"2012","journal-title":"J. Bacteriol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1128\/JB.06394-11","article-title":"BpaB and EbfC DNA-binding proteins regulate production of the Lyme disease spirochete\u2019s infection-associated Erp surface proteins","volume":"194","author":"Jutras","year":"2012","journal-title":"J. Bacteriol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1128\/IAI.70.2.491-497.2002","article-title":"Differential binding of host complement inhibitor factor H by Borrelia burgdorferi Erp surface proteins: A possible mechanism underlying the expansive host range of Lyme disease spirochetes","volume":"70","author":"Stevenson","year":"2002","journal-title":"Infect. Immun."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1128\/IAI.01133-08","article-title":"Borrelia burgdorferi infection-associated surface proteins ErpP, ErpA, and ErpC bind human plasminogen","volume":"77","author":"Brissette","year":"2009","journal-title":"Infect. Immun."},{"key":"ref_168","doi-asserted-by":"crossref","unstructured":"Stevenson, B., and Brissette, C.A. (2023). Erp and Rev adhesins of the Lyme disease spirochete\u2019s ubiquitous cp32 prophages assist the bacterium during vertebrate infection. Infect. Immun., 91.","DOI":"10.1128\/iai.00250-22"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.ijmm.2007.09.004","article-title":"Lyme borreliosis spirochete Erp proteins, their known host ligands, and potential roles in mammalian infection","volume":"298","author":"Brissette","year":"2008","journal-title":"Int. J. Med. Microbiol."},{"key":"ref_170","first-page":"152","article-title":"Immunological characterization of the complement regulator factor H-binding CRASP and Erp proteins of Borrelia burgdorferi","volume":"293","author":"Kraiczy","year":"2004","journal-title":"Int. J. Med. Microbiol. Suppl."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"5443","DOI":"10.1093\/nar\/gkq284","article-title":"BpaB, a novel protein encoded by the Lyme disease spirochete\u2019s cp32 prophages, binds to erp Operator 2 DNA","volume":"38","author":"Burns","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"4331","DOI":"10.1128\/JB.00005-06","article-title":"Borrelia burgdorferi EbfC, a novel, chromosomally encoded protein, binds specific DNA sequences adjacent to erp loci on the spirochete\u2019s resident cp32 prophages","volume":"188","author":"Babb","year":"2006","journal-title":"J. Bacteriol."},{"key":"ref_173","doi-asserted-by":"crossref","unstructured":"Jutras, B.L., Chenail, A.M., and Stevenson, B. (2017). Correction for Jutras et al., \"Changes in Bacterial Growth Rate Govern Expression of the Borrelia burgdorferi OspC and Erp Infection-Associated Surface Proteins\". J. Bacteriol., 199, Erratum in: J. Bacteriol. 2013, 195, 757\u2013764. https:\/\/doi.org\/10.1128\/JB.01956-12.","DOI":"10.1128\/JB.01956-12"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"4972","DOI":"10.1128\/IAI.73.8.4972-4981.2005","article-title":"Borrelia burgdorferi rel is responsible for generation of guanosine-3\u2032-diphosphate-5\u2032-triphosphate and growth control","volume":"73","author":"Bugrysheva","year":"2005","journal-title":"Infect. Immun."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1128\/JB.185.2.444-452.2003","article-title":"Expression of spoT in Borrelia burgdorferi during serum starvation","volume":"185","author":"Concepcion","year":"2003","journal-title":"J. Bacteriol."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1038\/nrmicro3448","article-title":"Recent functional insights into the role of (p) ppGpp in bacterial physiology","volume":"13","author":"Hauryliuk","year":"2015","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Drecktrah, D., Lybecker, M., Popitsch, N., Rescheneder, P., Hall, L.S., and Samuels, D.S. (2015). Correction: The Borrelia burgdorferi RelA\/SpoT Homolog and Stringent Response Regulate Survival in the Tick Vector and Global Gene Expression during Starvation. PLoS Pathog., 11, Erratum for: PLoS Pathog. 2015, 11, e1005160. https:\/\/doi.org\/10.1371\/journal.ppat.1005160.","DOI":"10.1371\/journal.ppat.1005160"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"7823","DOI":"10.1073\/pnas.0501170102","article-title":"DksA potentiates direct activation of amino acid promoters by ppGpp","volume":"102","author":"Paul","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1016\/j.molcel.2016.04.029","article-title":"ppGpp binding to a site at the RNAP-DksA interface accounts for its dramatic effects on transcription initiation during the stringent response","volume":"62","author":"Ross","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_180","doi-asserted-by":"crossref","unstructured":"Boyle, W.K., Groshong, A.M., Drecktrah, D., Boylan, J.A., Gherardini, F.C., Blevins, J.S., Samuels, D.S., and Bourret, T.J. (2019). DksA controls the response of the Lyme disease spirochete Borrelia burgdorferi to starvation. J. Bacteriol., 201.","DOI":"10.1128\/JB.00582-18"},{"key":"ref_181","doi-asserted-by":"crossref","unstructured":"PLOS ONE Staff (2015). Correction: Characterization of the RelBbu regulon in Borrelia burgdorferi reveals modu-lation of glycerol metabolism by (p)ppGpp. PLoS ONE, 10, Erratum in: PLoS ONE 2015, 10, e0118063. https:\/\/doi.org\/10.1371\/journal.pone.0118063.","DOI":"10.1371\/journal.pone.0118063"},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"5249","DOI":"10.1093\/nar\/gkv391","article-title":"New insights into the regulatory mechanisms of ppGpp and DksA on Escherichia coli RNA polymerase\u2013promoter complex","volume":"43","author":"Doniselli","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"ref_183","doi-asserted-by":"crossref","unstructured":"Gray, M.J. (2019). Inorganic polyphosphate accumulation in Escherichia coli is regulated by DksA but not by (p) ppGpp. J. Bacteriol., 201.","DOI":"10.1128\/JB.00664-18"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"5193","DOI":"10.1128\/JB.00330-07","article-title":"Identical, independent, and opposing roles of ppGpp and DksA in Escherichia coli","volume":"189","author":"Magnusson","year":"2007","journal-title":"J. Bacteriol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1111\/j.1365-2958.2010.07094.x","article-title":"Distinct roles of ppGpp and DksA in Legionella pneumophila differentiation","volume":"76","author":"Dalebroux","year":"2010","journal-title":"Mol. Microbiol."},{"key":"ref_186","doi-asserted-by":"crossref","unstructured":"Huang, C., Li, W., and Chen, J. (2023). Transcriptomic analysis reveals key roles of (p) ppGpp and DksA in regulating metabolism and chemotaxis in Yersinia enterocolitica. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24087612"},{"key":"ref_187","doi-asserted-by":"crossref","unstructured":"Huang, C., Meng, J., Li, W., and Chen, J. (2022). Similar and divergent roles of stringent regulator (p) ppGpp and DksA on pleiotropic phenotype of Yersinia enterocolitica. Microbiol. Spectr., 10.","DOI":"10.1128\/spectrum.02055-22"},{"key":"ref_188","doi-asserted-by":"crossref","unstructured":"Drecktrah, D., Hall, L.S., Rescheneder, P., Lybecker, M., and Samuels, D.S. (2018). The stringent response-regulated sRNA transcriptome of Borrelia burgdorferi. Front. Cell. Infect. Microbiol., 8.","DOI":"10.3389\/fcimb.2018.00231"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"2750","DOI":"10.1080\/21505594.2021.1995253","article-title":"Global regulator DksA modulates virulence of Acinetobacter baumannii","volume":"12","author":"Kim","year":"2021","journal-title":"Virulence"},{"key":"ref_190","doi-asserted-by":"crossref","unstructured":"Kim, N., Son, J.-H., Kim, K., Kim, H.-J., Shin, M., and Lee, J.-C. (2021). DksA modulates antimicrobial susceptibility of Acinetobacter baumannii. Antibiotics, 10.","DOI":"10.3390\/antibiotics10121472"},{"key":"ref_191","doi-asserted-by":"crossref","unstructured":"Chawla, M., Verma, J., Kumari, S., Matta, T., Senapati, T., Babele, P., Kumar, Y., Bhadra, R.K., and Das, B. (2025). (p) ppGpp and DksA play a crucial role in reducing the efficacy of \u03b2-lactam antibiotics by modulating bacterial membrane permeability. Microbiol. Spectr., 13.","DOI":"10.1128\/spectrum.01169-24"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"7035","DOI":"10.1093\/nar\/gkab491","article-title":"sRNA-mediated RNA processing regulates bacterial cell division","volume":"49","author":"Remes","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"1235","DOI":"10.1038\/s12276-024-01239-6","article-title":"Molecular insights into regulatory RNAs in the cellular machinery","volume":"56","author":"Yang","year":"2024","journal-title":"Exp. Mol. Med."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.1042\/BST20160363","article-title":"Impact of bacterial sRNAs in stress responses","volume":"45","author":"Holmqvist","year":"2017","journal-title":"Biochem. Soc. Trans."},{"key":"ref_195","doi-asserted-by":"crossref","unstructured":"Felden, B., and Cattoir, V. (2018). Bacterial adaptation to antibiotics through regulatory RNAs. Antimicrob. Agents Chemother., 62.","DOI":"10.1128\/AAC.02503-17"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1080\/10409238.2018.1473330","article-title":"Bacterial regulatory RNAs: Complexity, function, and putative drug targeting","volume":"53","author":"Cheah","year":"2018","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1128\/9781683670247.ch18","article-title":"Regulatory RNAs in virulence and host-microbe interactions","volume":"6","author":"Westermann","year":"2018","journal-title":"Regul. RNA Bact. Archaea"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.chembiol.2023.12.011","article-title":"Regulation of bacterial gene expression by non-coding RNA: It is all about time!","volume":"31","author":"Chauvier","year":"2024","journal-title":"Cell Chem. Biol."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1016\/j.tim.2022.03.007","article-title":"The emerging role of bacterial regulatory RNAs in disease","volume":"30","author":"Eichner","year":"2022","journal-title":"Trends Microbiol."},{"key":"ref_200","doi-asserted-by":"crossref","unstructured":"Chakravarty, S., and Mass\u00e9, E. (2019). RNA-dependent regulation of virulence in pathogenic bacteria. Front. Cell. Infect. Microbiol., 9.","DOI":"10.3389\/fcimb.2019.00337"},{"key":"ref_201","doi-asserted-by":"crossref","unstructured":"Menard, G., Silard, C., Suriray, M., Rouillon, A., and Augagneur, Y. (2022). Thirty years of sRNA-mediated regulation in Staphylococcus aureus: From initial discoveries to in vivo biological implications. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23137346"},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"10644","DOI":"10.1093\/nar\/gkab782","article-title":"A small regulatory RNA alters Staphylococcus aureus virulence by titrating RNAIII activity","volume":"49","author":"Gonzalez","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/1471-2164-10-165","article-title":"Small noncoding RNA GcvB is a novel regulator of acid resistance in Escherichia coli","volume":"10","author":"Jin","year":"2009","journal-title":"BMC Genom."},{"key":"ref_204","doi-asserted-by":"crossref","unstructured":"Ju, X., Fang, X., Xiao, Y., Li, B., Shi, R., Wei, C., and You, C. (2021). Small RNA GcvB regulates oxidative stress response of Escherichia coli. Antioxidants, 10.","DOI":"10.3390\/antiox10111774"},{"key":"ref_205","doi-asserted-by":"crossref","unstructured":"Popitsch, N., Bilusic, I., Rescheneder, P., Schroeder, R., and Lybecker, M. (2017). Temperature-dependent sRNA transcriptome of the Lyme disease spirochete. BMC Genom., 18.","DOI":"10.1186\/s12864-016-3398-3"},{"key":"ref_206","doi-asserted-by":"crossref","unstructured":"Arnold, W.K., Savage, C.R., Brissette, C.A., Seshu, J., Livny, J., and Stevenson, B. (2016). RNA-Seq of Borrelia burgdorferi in multiple phases of growth reveals insights into the dynamics of gene expression, transcriptome architecture, and noncoding RNAs. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0164165"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"3931","DOI":"10.1038\/s41467-023-39576-1","article-title":"Extensive diversity in RNA termination and regulation revealed by transcriptome mapping for the Lyme pathogen Borrelia burgdorferi","volume":"14","author":"Petroni","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"8472","DOI":"10.1128\/JB.186.24.8472-8477.2004","article-title":"The etiological agent of Lyme disease, Borrelia burgdorferi, appears to contain only a few small RNA molecules","volume":"186","author":"Ostberg","year":"2004","journal-title":"J. Bacteriol."},{"key":"ref_209","doi-asserted-by":"crossref","unstructured":"Medina-P\u00e9rez, D.N., Wager, B., Troy, E., Gao, L., Norris, S.J., Lin, T., Hu, L., Hyde, J.A., Lybecker, M., and Skare, J.T. (2020). The intergenic small non-coding RNA ittA is required for optimal infectivity and tissue tropism in Borrelia burgdorferi. PLoS Pathog., 16.","DOI":"10.1101\/2020.02.24.962522"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1038\/nrd.2018.93","article-title":"Principles for targeting RNA with drug-like small molecules","volume":"17","author":"Warner","year":"2018","journal-title":"Nat. Rev. Drug Discov."}],"container-title":["Microorganisms"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-2607\/13\/9\/2183\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T18:48:31Z","timestamp":1760035711000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-2607\/13\/9\/2183"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,9,18]]},"references-count":210,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2025,9]]}},"alternative-id":["microorganisms13092183"],"URL":"https:\/\/doi.org\/10.3390\/microorganisms13092183","relation":{},"ISSN":["2076-2607"],"issn-type":[{"value":"2076-2607","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,9,18]]}}}