{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T10:11:11Z","timestamp":1791108671605,"version":"4.1.0"},"reference-count":36,"publisher":"National Academy of Sciences","issue":"11","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2010,3,16]]},"abstract":"<jats:p>\n                    <jats:italic>Campylobacter jejuni<\/jats:italic>\n                    is the leading cause of acute bacterial diarrhea worldwide and is implicated in development of Guillain-Barr\u00e9 syndrome. Two major surface features, the outer membrane lipooligosaccharide and flagella, are highly variable and are often targets for modification. Presumably, these modifications provide a competitive advantage to the bacterium. In this work, we identify a gene encoding a phosphoethanolamine (pEtN) transferase (Cj0256) that serves a dual role in modifying not only the lipooligosaccharide lipid anchor lipid A with pEtN, but also the flagellar rod protein FlgG. Generation of a mutant in\n                    <jats:italic>C. jejuni<\/jats:italic>\n                    81\u2013176 by interruption of\n                    <jats:italic>cj0256<\/jats:italic>\n                    resulted in the absence of pEtN modifications on lipid A as well as FlgG. The\n                    <jats:italic>cj0256<\/jats:italic>\n                    mutant showed a 20-fold increase in sensitivity to the cationic antimicrobial peptide, polymyxin B, as well as a decrease in motility. Transmission EM of the\n                    <jats:italic>cj0256<\/jats:italic>\n                    mutant revealed a population (approximately 95%) lacking flagella, indicating that, without pEtN modification of FlgG, flagella production is hindered. Most intriguing, this research identifies a pEtN transferase showing preference for two periplasmic substrates linking membrane biogenesis and flagellar assembly. Cj0256 is a member of a large family of mostly uncharacterized proteins that may play a larger role in the decoration of bacterial surface structures.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0913451107","type":"journal-article","created":{"date-parts":[[2010,3,1]],"date-time":"2010-03-01T23:55:41Z","timestamp":1267487741000},"page":"5160-5165","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":100,"title":["A link between the assembly of flagella and lipooligosaccharide of the Gram-negative bacterium\n                    <i>Campylobacter jejuni<\/i>"],"prefix":"10.1073","volume":"107","author":[{"given":"Thomas W.","family":"Cullen","sequence":"first","affiliation":[{"name":"Section of Molecular Genetics and Microbiology and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. Stephen","family":"Trent","sequence":"additional","affiliation":[{"name":"Section of Molecular Genetics and Microbiology and"},{"name":"The Institute of Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2010,3]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1086\/381583"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.70.3.1202-1208.2002"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1039\/b808065h"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1177\/09680519060120040201"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.76.010307.145803"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1991.tb16036.x"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(90)90365-S"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M406480200"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M106962200"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M408106200"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2007.06044.x"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M108452200"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.178.11.3335-3338.1996"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00146-06"},{"key":"e_1_3_3_15_2","first-page":"159","article-title":"Cloning of EptA, the lipid A phosphoethanolamine transferase associated with polymyxin resistance","volume":"8","author":"Trent MS","year":"2002","unstructured":"MS Trent, CRH Raetz, Cloning of EptA, the lipid A phosphoethanolamine transferase associated with polymyxin resistance. 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