title: A link between the assembly of flagella and lipooligosaccharide of the Gram-negative bacterium Campylobacter jejuni.
abstract: Campylobacter jejuni is the leading cause of acute bacterial diarrhea worldwide and is implicated in development of Guillain-Barré 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 C. jejuni 81-176 by interruption of cj0256 resulted in the absence of pEtN modifications on lipid A as well as FlgG. The cj0256 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 cj0256 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.
authors.affiliation: Section of Molecular Genetics and Microbiology and The Institute of Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712, USA.
authors.forename: Thomas W
authors.initials: TW
authors.lastname: Cullen
authors.forename: M Stephen
authors.initials: MS
authors.lastname: Trent
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001426:Bacterial Proteins / Q000378:metabolism; D016123:Campylobacter jejuni / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D024881:Drug Resistance, Bacterial / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism; D004982:Ethanolaminephosphotransferase / Q000378:metabolism; D004983:Ethanolamines / Q000378:metabolism; D005407:Flagella / Q000187:drug effects / Q000378:metabolism*; D017353:Gene Deletion; D008050:Lipid A / Q000737:chemistry / Q000378:metabolism; D008070:Lipopolysaccharides / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D009068:Movement / Q000187:drug effects; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D004983:Ethanolamines; D008050:Lipid A; D008070:Lipopolysaccharides; C023023:lipid-linked oligosaccharides; C005448:phosphorylethanolamine; D004982:Ethanolaminephosphotransferase