ArticleThe Journal of biological chemistry2012
Characterization of unique modification of flagellar rod protein FlgG by Campylobacter jejuni lipid A phosphoethanolamine transferase, linking bacterial locomotion and antimicrobial peptide resistance.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
30 citing papers in PubMed, 47 citations in OpenAlex.
- Genomic insights into Campylobacter jejuni from Norwegian broilers: high genetic diversity and limited persistence on farms.BMC microbiology · 2026Article
- The dual functions of the GTPase BipA in ribosome assembly and surface structure biogenesis in Salmonella enterica serovar Typhimurium.PLoS pathogens · 2025Article
- The multifaceted roles of phosphoethanolamine-modified lipopolysaccharides: from stress response and virulence to cationic antimicrobial resistance.Microbiology and molecular biology reviews : MMBR · 2024Review
- Diacylglycerol Kinase A Is Essential for Polymyxin Resistance Provided by EptA, MCR-1, and Other Lipid A Phosphoethanolamine Transferases.Journal of bacteriology · 2022Article
- Remodeling of Lipid A inInternational journal of molecular sciences · 2022Article
- Zoonotic Transmission ofFrontiers in microbiology · 2022Article
- The bile salt deoxycholate inducesFrontiers in microbiology · 2022Article
- Mobile Colistin Resistance Enzyme MCR-3 Facilitates Bacterial Evasion of Host Phagocytosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- TheFrontiers in microbiology · 2020Article
- Role of Bacterial Cytoskeleton and Other Apparatuses in Cell Communication.Frontiers in molecular biosciences · 2020Review
- Definition of a Family of Nonmobile Colistin Resistance (NMCR-1) Determinants Suggests Aquatic Reservoirs for MCR-4.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019Article
- Proteomics Reveals Multiple Phenotypes Associated withMolecular & cellular proteomics : MCP · 2019Article
- Substrate Recognition by a Colistin Resistance Enzyme from Moraxella catarrhalis.ACS chemical biology · 2018Article
- Characterization of Two Novel Lipopolysaccharide Phosphoethanolamine Transferases in Pasteurella multocida and Their Role in Resistance to Cathelicidin-2.Infection and immunity · 2017Article
- Novel coordination of lipopolysaccharide modifications in Vibrio cholerae promotes CAMP resistance.Molecular microbiology · 2017Article
- Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- High resolution crystal structure of the catalytic domain of MCR-1.Scientific reports · 2016Article
- Polymyxin: Alternative Mechanisms of Action and Resistance.Cold Spring Harbor perspectives in medicine · 2016Review
- On the in vivo significance of bacterial resistance to antimicrobial peptides.Biochimica et biophysica acta · 2015Review
- Kdo2 -lipid A: structural diversity and impact on immunopharmacology.Biological reviews of the Cambridge Philosophical Society · 2015Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 4 countries.
Funding
Abstract
Gram-negative bacteria assemble complex surface structures that interface with the surrounding environment and are involved in pathogenesis. Recent work in Campylobacter jejuni identified a gene encoding a novel phosphoethanolamine (pEtN) transferase Cj0256, renamed EptC, that serves a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain of C. jejuni lipooligosaccharide with a pEtN residue. In this work, we characterize the unique post-translational pEtN modification of FlgG using collision-induced and electron transfer dissociation mass spectrometry, as well as a genetic approach using site-directed mutagenesis to determine the site of modification. Specifically, we show that FlgG is modified with pEtN at a single site (Thr(75)) by EptC and demonstrate enzyme specificity by showing that EptC is unable to modify other amino acids (e.g. serine and tyrosine). Using Campylobacter strains expressing site-directed FlgG mutants, we also show that defects in motility arise directly from the loss of pEtN modification of FlgG. Interestingly, alignments of FlgG from most epsilon proteobacteria reveal a conserved site of modification. Characterization of EptC and its enzymatic targets expands on the increasingly important field of prokaryotic post-translational modification of bacterial surface structures and the unidentified role they may play in pathogenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.