{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T10:28:19Z","timestamp":1740133699722,"version":"3.37.3"},"reference-count":56,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2016,2,15]],"date-time":"2016-02-15T00:00:00Z","timestamp":1455494400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000060","name":"HHS | NIH | National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["AI078958"],"award-info":[{"award-number":["AI078958"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000072","name":"HHS | NIH | National Institute of Dental and Craniofacial Research","doi-asserted-by":"publisher","award":["DE023431"],"award-info":[{"award-number":["DE023431"]}],"id":[{"id":"10.13039\/100000072","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006492","name":"Division of Intramural Research, National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["AI087946"],"award-info":[{"award-number":["AI087946"]}],"id":[{"id":"10.13039\/100006492","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2016,2,15]]},"abstract":"ABSTRACT<\/jats:title>\n \n The Lyme disease spirochete\n Borrelia burgdorferi<\/jats:named-content>\n has five putative methyl-accepting chemotaxis proteins (MCPs). In this report, we provide evidence that a hypothetical protein, BB0569, is essential for the chemotaxis of\n B. burgdorferi<\/jats:named-content>\n . While BB0569 lacks significant homology to the canonical MCPs, it contains a conserved domain (spanning residues 110 to 170) that is often evident in membrane-bound MCPs such as Tar and Tsr of\n Escherichia coli<\/jats:named-content>\n . Unlike Tar and Tsr, BB0569 lacks transmembrane regions and recognizable HAMP and methylation domains and is similar to TlpC, a cytoplasmic chemoreceptor of\n Rhodobacter sphaeroides<\/jats:named-content>\n . An isogenic mutant of\n BB0569<\/jats:italic>\n constantly runs in one direction and fails to respond to attractants, indicating that BB0569 is essential for chemotaxis. Immunofluorescence, green fluorescent protein (GFP) fusion, and cryo-electron tomography analyses demonstrate that BB0569 localizes at the cell poles and is required for chemoreceptor clustering at the cell poles. Protein cross-linking studies reveal that BB0569 forms large protein complexes with MCP3, indicative of its interactions with other MCPs. Interestingly, analysis of\n B. burgdorferi<\/jats:named-content>\n mcp<\/jats:italic>\n mutants shows that inactivation of either\n mcp<\/jats:italic>\n 2<\/jats:sub>\n or\n mcp<\/jats:italic>\n 3<\/jats:sub>\n reduces the level of BB0569 substantially and that such a reduction is caused by protein turnover. Collectively, these results demonstrate that the domain composition and function of BB0569 are similar in some respects to those of TlpC but that these proteins are different in their cellular locations, further highlighting that the chemotaxis of\n B. burgdorferi<\/jats:named-content>\n is unique and different from the\n Escherichia coli<\/jats:named-content>\n and\n Salmonella enterica<\/jats:named-content>\n paradigm.\n <\/jats:p>\n \n IMPORTANCE<\/jats:bold>\n Spirochete chemotaxis differs substantially from the\n Escherichia coli<\/jats:named-content>\n and\n Salmonella enterica<\/jats:named-content>\n paradigm, and the basis for controlling the rotation of the bundles of periplasmic flagella at each end of the cell is unknown. In recent years,\n Borrelia burgdorferi<\/jats:named-content>\n , the causative agent of Lyme disease, has been used as a model organism to understand spirochete chemotaxis and its role in infectious processes of the disease. In this report, BB0569, a hypothetical protein of\n B. burgdorferi<\/jats:named-content>\n , has been investigated by using an approach of genetic, biochemistry, and cryo-electron tomography analyses. The results indicate that BB0569 has a distinct role in chemotaxis that may be unique to spirochetes and represents a novel paradigm.\n <\/jats:p>","DOI":"10.1128\/jb.00877-15","type":"journal-article","created":{"date-parts":[[2015,12,8]],"date-time":"2015-12-08T15:05:40Z","timestamp":1449587140000},"page":"664-672","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":12,"title":["Hypothetical Protein BB0569 Is Essential for Chemotaxis of the Lyme Disease Spirochete Borrelia burgdorferi"],"prefix":"10.1128","volume":"198","author":[{"given":"Kai","family":"Zhang","sequence":"first","affiliation":[{"name":"Department of Oral Biology, The State University of New York at Buffalo, Buffalo, New York, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jun","family":"Liu","sequence":"additional","affiliation":[{"name":"Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, Houston, Texas, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nyles W.","family":"Charon","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Cell Biology, Health Sciences Center, West Virginia University, Morgantown, West Virginia, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chunhao","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Oral Biology, The State University of New York at Buffalo, Buffalo, New York, USA"},{"name":"Department of Microbiology and Immunology, The State University of New York at Buffalo, Buffalo, New York, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.153.3737.708"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bb.04.060175.001003"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrm1524"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibs.2007.09.014"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro2505"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1104824108"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(92)90247-A"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.ge.11.120177.002145"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.151.1.106-113.1982"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.8456299"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0905181106"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1200781109"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1038\/23512"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0806401105"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.112408.134215"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0506040102"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.092071899"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2002.03252.x"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tim.2008.02.006"},{"key":"e_1_3_3_21_2","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1038\/264577a0","article-title":"Operon controlling motility and chemotoxis in E. coli","volume":"264","author":"Silverman M","year":"1976","unstructured":"Silverman M, Simon M. 1976. 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