{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T01:28:24Z","timestamp":1789522104496,"version":"build-2803163510"},"reference-count":62,"publisher":"Public Library of Science (PLoS)","issue":"4","license":[{"start":{"date-parts":[[2024,4,16]],"date-time":"2024-04-16T00:00:00Z","timestamp":1713225600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100005375","name":"Latvian Council of Science","doi-asserted-by":"crossref","award":["lzp-2021\/1-0068"],"award-info":[{"award-number":["lzp-2021\/1-0068"]}],"id":[{"id":"10.13039\/501100005375","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"abstract":"<jats:p>Lyme disease is the most prevalent vector-borne infectious disease in Europe and the USA. <jats:italic>Borrelia burgdorferi<\/jats:italic>, as the causative agent of Lyme disease, is transmitted to the mammalian host during the tick blood meal. To adapt to the different encountered environments, <jats:italic>Borrelia<\/jats:italic> has adjusted the expression pattern of various, mostly outer surface proteins. The function of most <jats:italic>B<\/jats:italic>. <jats:italic>burgdorferi<\/jats:italic> outer surface proteins remains unknown. We determined the crystal structure of a previously uncharacterized <jats:italic>B<\/jats:italic>. <jats:italic>burgdorferi<\/jats:italic> outer surface protein BBK01, known to belong to the paralogous gene family 12 (PFam12) as one of its five members. PFam12 members are shown to be upregulated as the tick starts its blood meal. Structural analysis of BBK01 revealed similarity to the coiled coil domain of structural maintenance of chromosomes (SMC) protein family members, while functional studies indicated that all PFam12 members are non-specific DNA-binding proteins. The residues involved in DNA binding were identified and probed by site-directed mutagenesis. The combination of SMC-like proteins being attached to the outer membrane and exposed to the environment or located in the periplasm, as observed in the case of PFam12 members, and displaying the ability to bind DNA, represents a unique feature previously not observed in bacteria.<\/jats:p>","DOI":"10.1371\/journal.pone.0296127","type":"journal-article","created":{"date-parts":[[2024,4,16]],"date-time":"2024-04-16T18:02:11Z","timestamp":1713290531000},"page":"e0296127","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":8,"title":["Members of the paralogous gene family 12 from the Lyme disease agent Borrelia burgdorferi are non-specific DNA-binding 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Microbiol"},{"key":"pone.0296127.ref011","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1016\/j.bbamcr.2014.04.022","article-title":"Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond","volume":"1843","author":"WR Zuckert","year":"2014","journal-title":"Biochim Biophys Acta"},{"key":"pone.0296127.ref012","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1099\/00221287-146-7-1491","article-title":"Spirochaetal lipoproteins and pathogenesis","volume":"146","author":"DA Haake","year":"2000","journal-title":"Microbiology"},{"key":"pone.0296127.ref013","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1046\/j.1365-2958.2000.01698.x","article-title":"A bacterial genome in flux: the twelve linear and nine circular extrachromosomal DNAs in an infectious isolate of the Lyme disease spirochete Borrelia burgdorferi","volume":"35","author":"S Casjens","year":"2000","journal-title":"Mol 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Yang","year":"2013","journal-title":"Microbes Infect"},{"key":"pone.0296127.ref020","doi-asserted-by":"crossref","first-page":"2910","DOI":"10.1128\/IAI.00372-10","article-title":"Role of the surface lipoprotein BBA07 in the enzootic cycle of Borrelia burgdorferi","volume":"78","author":"H Xu","year":"2010","journal-title":"Infect Immun"},{"key":"pone.0296127.ref021","doi-asserted-by":"crossref","first-page":"e1002079","DOI":"10.1371\/journal.ppat.1002079","article-title":"Molecular interactions that enable movement of the Lyme disease agent from the tick gut into the hemolymph","volume":"7","author":"L Zhang","year":"2011","journal-title":"PLoS Pathog"},{"key":"pone.0296127.ref022","doi-asserted-by":"crossref","first-page":"e33280","DOI":"10.1371\/journal.pone.0033280","article-title":"Genome stability of Lyme disease spirochetes: comparative genomics of Borrelia burgdorferi plasmids","volume":"7","author":"SR Casjens","year":"2012","journal-title":"PLoS 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A"},{"key":"pone.0296127.ref026","doi-asserted-by":"crossref","first-page":"6677","DOI":"10.1128\/IAI.68.12.6677-6684.2000","article-title":"Identification of 11 pH-regulated genes in Borrelia burgdorferi localizing to linear plasmids","volume":"68","author":"JA Carroll","year":"2000","journal-title":"Infect Immun"},{"key":"pone.0296127.ref027","doi-asserted-by":"crossref","first-page":"e0036422","DOI":"10.1128\/iai.00364-22","article-title":"FtlA and FtlB Are Candidates for Inclusion in a Next-Generation Multiantigen Subunit Vaccine for Lyme Disease","volume":"90","author":"AC Camire","year":"2022","journal-title":"Infect Immun"},{"key":"pone.0296127.ref028","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1038\/nmeth.1701","article-title":"SignalP 4.0: discriminating signal peptides from transmembrane regions","volume":"8","author":"TN Petersen","year":"2011","journal-title":"Nat 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Crystallogr"},{"key":"pone.0296127.ref032","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Xds","volume":"66","author":"W Kabsch","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"pone.0296127.ref033","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1107\/S0108767307043930","article-title":"A short history of SHELX","volume":"64","author":"GM Sheldrick","year":"2008","journal-title":"Acta Crystallogr A"},{"key":"pone.0296127.ref034","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1107\/S0907444906022116","article-title":"The Buccaneer software for automated model building. 1. Tracing protein chains","volume":"62","author":"K Cowtan","year":"2006","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"pone.0296127.ref035","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"P Emsley","year":"2004","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"pone.0296127.ref036","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"GN Murshudov","year":"1997","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"pone.0296127.ref037","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"J Jumper","year":"2021","journal-title":"Nature"},{"key":"pone.0296127.ref038","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.ttbdis.2013.09.005","article-title":"Crystal structure of the infectious phenotype-associated outer surface protein BBA66 from the Lyme disease agent Borrelia burgdorferi","volume":"5","author":"K Brangulis","year":"2014","journal-title":"Ticks Tick Borne Dis"},{"key":"pone.0296127.ref039","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1002\/pro.3280","article-title":"Improvements to the APBS biomolecular solvation software suite","volume":"27","author":"E Jurrus","year":"2018","journal-title":"Protein Sci"},{"key":"pone.0296127.ref040","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"E Krissinel","year":"2007","journal-title":"J Mol Biol"},{"key":"pone.0296127.ref041","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1107\/S0907444904026460","article-title":"Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions","volume":"60","author":"E Krissinel","year":"2004","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"pone.0296127.ref042","doi-asserted-by":"crossref","first-page":"2780","DOI":"10.1093\/bioinformatics\/btn507","article-title":"Searching protein structure databases with DaliLite v.3","volume":"24","author":"L Holm","year":"2008","journal-title":"Bioinformatics"},{"key":"pone.0296127.ref043","doi-asserted-by":"crossref","DOI":"10.1186\/gb-2002-3-2-reviews3003","article-title":"Structural maintenance of chromosomes (SMC) proteins, a family of conserved ATPases","volume":"3","author":"SH Harvey","year":"2002","journal-title":"Genome Biol"},{"key":"pone.0296127.ref044","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1101\/gad.1320505","article-title":"Dynamic molecular linkers of the genome: the first decade of SMC proteins","volume":"19","author":"A Losada","year":"2005","journal-title":"Genes Dev"},{"key":"pone.0296127.ref045","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.molcel.2017.06.010","article-title":"Structure of Full-Length SMC and Rearrangements Required for Chromosome Organization","volume":"67","author":"ML Diebold-Durand","year":"2017","journal-title":"Mol Cell"},{"key":"pone.0296127.ref046","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1016\/j.molcel.2014.11.023","article-title":"Molecular basis for SMC rod formation and its dissolution upon DNA binding","volume":"57","author":"YM Soh","year":"2015","journal-title":"Mol Cell"},{"key":"pone.0296127.ref047","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.molcel.2005.11.026","article-title":"Opening closed arms: long-distance activation of SMC ATPase by hinge-DNA interactions","volume":"21","author":"M Hirano","year":"2006","journal-title":"Mol Cell"},{"key":"pone.0296127.ref048","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":"CM Fraser","year":"1997","journal-title":"Nature"},{"key":"pone.0296127.ref049","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/msb.2011.75","article-title":"Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega","volume":"7","author":"F Sievers","year":"2011","journal-title":"Mol Syst Biol"},{"key":"pone.0296127.ref050","doi-asserted-by":"crossref","first-page":"W320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering key features in protein structures with the new ENDscript server","volume":"42","author":"X Robert","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"pone.0296127.ref051","doi-asserted-by":"crossref","first-page":"W5","DOI":"10.1093\/nar\/gkn201","article-title":"NCBI BLAST: a better web interface","volume":"36","author":"M Johnson","year":"2008","journal-title":"Nucleic Acids Res"},{"key":"pone.0296127.ref052","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1016\/j.jmb.2004.03.016","article-title":"A combined transmembrane topology and signal peptide prediction method","volume":"338","author":"L Kall","year":"2004","journal-title":"J Mol Biol"},{"key":"pone.0296127.ref053","doi-asserted-by":"crossref","first-page":"W401","DOI":"10.1093\/nar\/gkv485","article-title":"The TOPCONS web server for consensus prediction of membrane protein topology and signal peptides","volume":"43","author":"KD Tsirigos","year":"2015","journal-title":"Nucleic Acids Res"},{"key":"pone.0296127.ref054","doi-asserted-by":"crossref","first-page":"1829","DOI":"10.1038\/s41596-020-0312-x","article-title":"The HDOCK server for integrated protein-protein docking","volume":"15","author":"Y Yan","year":"2020","journal-title":"Nat Protoc"},{"key":"pone.0296127.ref055","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1128\/IAI.01156-10","article-title":"BB0844, an RpoS-regulated protein, is dispensable for Borrelia burgdorferi infectivity and maintenance in the mouse-tick infectious cycle","volume":"79","author":"S Banik","year":"2011","journal-title":"Infect Immun"},{"key":"pone.0296127.ref056","doi-asserted-by":"crossref","first-page":"e01667","DOI":"10.1128\/mBio.01667-14","article-title":"The extracellular matrix of Staphylococcus aureus biofilms comprises cytoplasmic proteins that associate with the cell surface in response to 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