ArticleThe Journal of cell biology1998
A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 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
70 citing papers in PubMed, 216 citations in OpenAlex.
- Article
- Overview of Bacterial Protein Toxins from Pathogenic Bacteria: Mode of Action and Insights into Evolution.Toxins · 2024Review
- Patch repair protects cells from the small pore-forming toxin aerolysin.Journal of cell science · 2023Article
- Beyond pore formation: reorganization of the plasma membrane induced by pore-forming proteins.Cellular and molecular life sciences : CMLS · 2021Review
- Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021Review
- Microparticle Encapsulation of a Prostate-targeted Biologic for the Treatment of Liver Metastases in a Preclinical Model of Castration-resistant Prostate Cancer.Molecular cancer therapeutics · 2020Article
- Mammalian membrane trafficking as seen through the lens of bacterial toxins.Cellular microbiology · 2020Review
- Proteomic characterization and discrimination of Aeromonas species recovered from meat and water samples with a spotlight on the antimicrobial resistance of Aeromonas hydrophila.MicrobiologyOpen · 2019Article
- Single-molecule sensing of peptides and nucleic acids by engineered aerolysin nanopores.Nature communications · 2019Article
- Article
- Mechanisms protecting host cells against bacterial pore-forming toxins.Cellular and molecular life sciences : CMLS · 2019Review
- Anthrax toxin requires ZDHHC5-mediated palmitoylation of its surface-processing host enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural basis of Toxoplasma gondii perforin-like protein 1 membrane interaction and activity during egress.PLoS pathogens · 2018Article
- Glycosyl-Phosphatidylinositol-Anchored Anti-HIV Env Single-Chain Variable Fragments Interfere with HIV-1 Env Processing and Viral Infectivity.Journal of virology · 2018Article
- Hostile intruder: Toxoplasma holds host organelles captive.PLoS pathogens · 2018Article
- Molecular switching system using glycosylphosphatidylinositol to select cells highly expressing recombinant proteins.Scientific reports · 2017Article
- Synthesis of biotin-labelled core glycans of GPI anchors and their application in the study of GPI interaction with pore-forming bacterial toxins.Chemical communications (Cambridge, England) · 2017Article
- Toxoplasma gondii immune mapped protein 1 is anchored to the inner leaflet of the plasma membrane and adopts a novel protein fold.Biochimica et biophysica acta. Proteins and proteomics · 2017Article
- Endoplasmic reticulum chaperone Gp96 controls actomyosin dynamics and protects against pore-forming toxins.EMBO reports · 2017Article
- Cytoplasmic vacuolization in cell death and survival.Oncotarget · 2016Review
10 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
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this paper, we have investigated the effects of the pore-forming toxin aerolysin, produced by Aeromonas hydrophila, on mammalian cells. Our data indicate that the protoxin binds to an 80-kD glycosyl-phosphatidylinositol (GPI)-anchored protein on BHK cells, and that the bound toxin is associated with specialized plasma membrane domains, described as detergent-insoluble microdomains, or cholesterol-glycolipid "rafts." We show that the protoxin is then processed to its mature form by host cell proteases. We propose that the preferential association of the toxin with rafts, through binding to GPI-anchored proteins, is likely to increase the local toxin concentration and thereby promote oligomerization, a step that it is a prerequisite for channel formation. We show that channel formation does not lead to disruption of the plasma membrane but to the selective permeabilization to small ions such as potassium, which causes plasma membrane depolarization. Next we studied the consequences of channel formation on the organization and dynamics of intracellular membranes. Strikingly, we found that the toxin causes dramatic vacuolation of the ER, but does not affect other intracellular compartments. Concomitantly we find that the COPI coat is released from biosynthetic membranes and that biosynthetic transport of newly synthesized transmembrane G protein of vesicular stomatitis virus is inhibited. Our data indicate that binding of proaerolysin to GPI-anchored proteins and processing of the toxin lead to oligomerization and channel formation in the plasma membrane, which in turn causes selective disorganization of early biosynthetic membrane dynamics.
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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.