Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: diarrhea [ICD11:
ME05.1 
, ICD11:
SA55 ];
infection due to Campylobacter jejuni [ICD11:
XN4Q5 ]
The structure was elucidated in this paperNCBI PubMed ID: 20194750Publication DOI: 10.1073/pnas.0913451107Journal NLM ID: 7505876Publisher: National Academy of Sciences
Correspondence: strent
mail.utexas.edu
Institutions: Section of Molecular Genetics and Microbiology and The Institute of Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712, USA
Campylobacter jejuni is the leading cause of acute bacterial diarrhea worldwide and is implicated in development of Guillain-Barre 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.
Lipooligosaccharide, lipid A, Campylobacter jejuni, cell envelope, motility, antimicrobial peptides
Structure type: oligomer ; 1921.4 [M-H]-
Location inside paper: p.5162, fig.3
Compound class: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_141181
Methods: PCR, SDS-PAGE, MALDI-TOF MS, genetic methods, motility assays
Comments, role: Campylobacter jejuni wild type strain 87-176 and mutant strain 81-176B (Δcj0256, cj0256+)
Related record ID(s): 25222, 31991, 31992, 31993
NCBI Taxonomy refs (TaxIDs): 354242
Show glycosyltransferases
There is only one chemically distinct structure:
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(later renamed to: Campylobacter jejuni subsp. jejuni 81-176)