ArticleThe Journal of biological chemistry2002
Bacterial surface association of heat-labile enterotoxin through lipopolysaccharide after secretion via the general secretory pathway.
Article in The Journal of biological chemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
What it found
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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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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.
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Who cites it
84 citing papers in PubMed, 158 citations in OpenAlex.
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- Bacterial extracellular vesicles in osteoarthritis: a new bridge of the gut-joint axis.Gut microbes · 2025Review
- The Type II Secretion System Utilizes AsmA-like Protein GspN to Facilitate Transport of Lipoproteins to the Cell Surface inbioRxiv : the preprint server for biology · 2025Article
- A RecombinantInternational journal of molecular sciences · 2024Article
- Microbiota-Derived Extracellular Vesicle as Emerging Actors in Host Interactions.International journal of molecular sciences · 2024Review
- UsingBiochemistry · 2024Article
- Extracellular Vesicles and Bacteriophages: New Directions in Environmental Biocolloid Research.Environmental science & technology · 2023Review
- UsingbioRxiv : the preprint server for biology · 2023Article
- The Immunogenicity and Properties of a Whole-Cell ETEC Vaccine Inactivated with Psoralen and UVA Light in Comparison to Formalin.Microorganisms · 2023Article
- Membrane translocation process revealed by in situ structures of type II secretion system secretins.Nature communications · 2023Article
- What's gut got to do with it? The role of the microbiota and inflammation in the development of adiposity and obesity.Immunometabolism (Cobham, Surrey) · 2023Review
- Composition and functions of bacterial membrane vesicles.Nature reviews. Microbiology · 2023Review
- The Two Faces of Bacterial Membrane Vesicles: Pathophysiological Roles and Therapeutic Opportunities.Antibiotics (Basel, Switzerland) · 2023Review
- Emerging role of bacterial outer membrane vesicle in gastrointestinal tract.Gut pathogens · 2023Review
- Review
- Both LTA and LTB Subunits Are Equally Important to Heat-Labile Enterotoxin (LT)-Enhanced Bacterial Adherence.International journal of molecular sciences · 2023Article
- Review
- Heat-Labile Toxin from EnterotoxigenicToxins · 2021Article
24 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Heat-labile enterotoxin (LT) is an important virulence factor expressed by enterotoxigenic Escherichia coli. The route of LT secretion through the outer membrane and the cellular and extracellular localization of secreted LT were examined. Using a fluorescently labeled receptor, LT was found to be specifically secreted onto the surface of wild type enterotoxigenic Escherichia coli. The main terminal branch of the general secretory pathway (GSP) was necessary and sufficient to localize LT to the bacterial surface in a K-12 strain. LT is a heteromeric toxin, and we determined that its cell surface localization was mediated by the its B subunit independent of an intact G(M1) ganglioside binding site and that LT binds lipopolysaccharide and G(M1) concurrently. The majority of LT secreted into the culture supernatant by the GSP in E. coli associated with vesicles. Only a mutation in hns, not overexpression of the GSP or LT, caused an increase in vesicle yield, supporting a specific vesicle formation machinery regulated by the nucleoid-associated protein HNS. We propose a model in which LT is secreted by the GSP across the outer membrane, secreted LT binds lipopolysaccharide via a G(M1)-independent binding region on its B subunit, and LT on the surface of released outer membrane vesicles interacts with host cell receptors, leading to intoxication. These data explain a novel mechanism of vesicle-mediated receptor-dependent delivery of a bacterial toxin into a host cell.
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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.