ArticleThe FEBS journal2011
Membrane interaction of Pasteurella multocida toxin involves sphingomyelin.
Article in The FEBS journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 22 citations in OpenAlex.
- Bacterial Toxin Exploits Host Membrane Phospholipid as a Receptor for Binding, Entry, and Cytopathogenicity.Molecular microbiology · 2026Article
- Anthrax Toxin: A Pioneer of Targeted Protein Toxins.Toxins · 2025Review
- Some Examples of Bacterial Toxins as Tools.Toxins · 2024Review
- Revealing the lethal effects ofFrontiers in microbiology · 2024Article
- Genome wide CRISPR screen for Pasteurella multocida toxin (PMT) binding proteins reveals LDL Receptor Related Protein 1 (LRP1) as crucial cellular receptor.PLoS pathogens · 2022Article
- Pasteurella multocida toxin - lessons learned from a mitogenic toxin.Frontiers in immunology · 2022Review
- In Vivo Targets ofInternational journal of molecular sciences · 2020Article
- Cytosolic Delivery of Multidomain Cargos by the N Terminus of Pasteurella multocida Toxin.Infection and immunity · 2018Article
- The membrane localization domains of two distinct bacterial toxins form a 4-helix-bundle in solution.Protein science : a publication of the Protein Society · 2017Article
- Selective Membrane Redistribution and Depletion of Gαq-Protein by Pasteurella multocida Toxin.Toxins · 2016Article
- Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin.Biomolecular NMR assignments · 2014Article
- The actions of Pasteurella multocida toxin on neuronal cells.Neuropharmacology · 2014Article
- Pasteurella multocida toxin as a transporter of non-cell-permeating proteins.Infection and immunity · 2013Article
- Determinants of pH-dependent modulation of translocation in dermonecrotic G-protein-deamidating toxins.Toxins · 2013Article
- Pasteurella multocida toxin (PMT) upregulates CTGF which leads to mTORC1 activation in Swiss 3T3 cells.Cellular signalling · 2013Article
- Mammalian target of rapamycin complex 1 (mTORC1) plays a role in Pasteurella multocida toxin (PMT)-induced protein synthesis and proliferation in Swiss 3T3 cells.The Journal of biological chemistry · 2013Article
- Pasteurella multocida toxin interaction with host cells: entry and cellular effects.Current topics in microbiology and immunology · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 1 institution in 1 country.
Funding
Abstract
Pasteurella multocida toxin (PMT) is an AB toxin that causes pleiotropic effects in targeted host cells. The N-terminus of PMT (PMT-N) is considered to harbor the membrane receptor binding and translocation domains responsible for mediating cellular entry and delivery of the C-terminal catalytic domain into the host cytosol. Previous studies have implicated gangliosides as the host receptors for PMT binding. To gain further insight into the binding interactions involved in PMT binding to cell membranes, we explored the role of various membrane components in PMT binding, utilizing four different approaches: (a) TLC-overlay binding experiments with (125) I-labeled PMT, PMT-N or the C-terminus of PMT; (b) pull-down experiments using reconstituted membrane liposomes with full-length PMT; (c) surface plasmon resonance analysis of PMT-N binding to reconstituted membrane liposomes; (d) and surface plasmon resonance analysis of PMT-N binding to HEK-293T cell membranes without or with sphingomyelinase, phospholipase D or trypsin treatment. The results obtained revealed that, in our experimental system, full-length PMT and PMT-N did not bind to gangliosides, including monoasialogangliosides GM(1) , GM(2) or GM(3) , but instead bound to membrane phospholipids, primarily the abundant sphingophospholipid sphingomyelin or phosphatidylcholine with other lipid components. Collectively, these studies demonstrate the importance of sphingomyelin for PMT binding to membranes and suggest the involvement of a protein co-receptor.
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.