ArticleThe Journal of biological chemistry2004
Lipopolysaccharide 3-deoxy-D-manno-octulosonic acid (Kdo) core determines bacterial association of secreted toxins.
Article in The Journal of biological chemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 69 citations in OpenAlex.
- Evaluation of Vibrio natriegens as a fast-growing alternative host for plasmid DNA production.Microbial cell factories · 2026Article
- UsingBiochemistry · 2024Article
- Extracellular Vesicles and Bacteriophages: New Directions in Environmental Biocolloid Research.Environmental science & technology · 2023Review
- UsingbioRxiv : the preprint server for biology · 2023Article
- The Two Faces of Bacterial Membrane Vesicles: Pathophysiological Roles and Therapeutic Opportunities.Antibiotics (Basel, Switzerland) · 2023Review
- Outer Membrane Vesicles: Biogenesis, Functions, and Issues.Microbiology and molecular biology reviews : MMBR · 2022Review
- The extracellular vesicle generation paradox: a bacterial point of view.The EMBO journal · 2021Review
- An AttenuatedFrontiers in veterinary science · 2020Article
- Outer Membrane Interaction Kinetics of New Polymyxin B Analogs in Gram-Negative Bacilli.Antimicrobial agents and chemotherapy · 2019Article
- Pushing the envelope: LPS modifications and their consequences.Nature reviews. Microbiology · 2019Review
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- Review of Newly Identified Functions Associated With the Heat-Labile Toxin of EnterotoxigenicFrontiers in cellular and infection microbiology · 2019Review
- Intestinal challenge with enterotoxigenicAnimal nutrition (Zhongguo xu mu shou yi xue hui) · 2017Review
- Phylogeny ofFrontiers in microbiology · 2017Article
- Animal Enterotoxigenic Escherichia coli.EcoSal Plus · 2016Review
- Novel GM1 ganglioside-like peptide mimics prevent the association of cholera toxin to human intestinal epithelial cells in vitro.Glycobiology · 2016Article
- Protein selection and export via outer membrane vesicles.Biochimica et biophysica acta · 2014Review
- A divergent Pseudomonas aeruginosa palmitoyltransferase essential for cystic fibrosis-specific lipid A.Molecular microbiology · 2014Article
- Fortifying the barrier: the impact of lipid A remodelling on bacterial pathogenesis.Nature reviews. Microbiology · 2013Review
- Instability of toxin A subunit of AB(5) toxins in the bacterial periplasm caused by deficiency of their cognate B subunits.Biochimica et biophysica acta · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In contrast to cholera toxin (CT), which is secreted solubly by Vibrio cholerae across the outer membrane, heat-labile enterotoxin (LT) is retained on the surface of enterotoxigenic Escherichia coli (ETEC) via an interaction with lipopolysaccharide (LPS). We examined the nature of the association between LT and LPS. Soluble LT binds to the surface of LPS deep-rough biosynthesis mutants but not to lipid A, indicating that only the Kdo (3-deoxy-d-manno-octulosonic acid) core is required for binding. Although capable of binding truncated LPS and Kdo, LT has a higher affinity for longer, more complete LPS species. A putative LPS binding pocket is proposed based on the crystal structure of the toxin. The ability to bind LPS and remain associated with the bacterial surface is not unique to LT, as CT also binds to E. coli LPS. However, neither LT nor CT is capable of binding to the surface of Vibrio. The core structures of Vibrio and E. coli LPS differ in that Vibrio contains a phosphorylated single Kdo-lipid A, and E. coli LPS contains unphosphorylated Kdo2-lipid A. We determined that the phosphate group on the Kdo core of Vibrio LPS prevents CT from binding, resulting in the secretion of soluble toxin. Because LT binds E. coli LPS, it remains associated with the extracellular bacterial surface and is released in association with outer membrane vesicles. We propose that difference in the extracellular fates of LT and CT contribute to the differences in disease caused by ETEC and Vibrio cholerae.
Indexed as
Identifiers
What OpenQuestion holds
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.