ArticleCellular and molecular life sciences : CMLS2021
The Gb3-enriched CD59/flotillin plasma membrane domain regulates host cell invasion by Pseudomonas aeruginosa.
Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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.
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
21 citing papers in PubMed, 1 synthesis or guideline pooled it, 32 citations in OpenAlex.
- Molecular exploration of host-pathogen interactions in severeFrontiers in medicine · 2025Pooled it
- Photoisomerizing molecules in biological membranes.Nature reviews. Chemistry · 2026Review
- Role of Flotillin-1 In Listeria monocytogenes Cell-to-Cell Spreading.The Journal of infectious diseases · 2025Article
- Cross-membrane cooperation among bacteria can facilitate intracellular pathogenesis.Nature communications · 2025Article
- Globotriaosylceramide as a potential biomarker for auxiliary detection of lower respiratory tract infections ofExperimental and therapeutic medicine · 2025Article
- Lectin-Based Substrate Detection in Fabry Disease Using the Gb3-Binding Lectins StxB and LecA.International journal of molecular sciences · 2025Article
- The BacteriumBiomolecules · 2025Article
- Evidence for intracellularJournal of bacteriology · 2024Review
- Translocation across a human enteroid monolayer by zoonoticiScience · 2024Article
- A Patching and Coding Lipid Raft-Localized Universal Imaging Platform.Chemical & biomedical imaging · 2024Article
- Subversion of the Complement System by Pseudomonas aeruginosa.Journal of bacteriology · 2023Review
- Current concepts on Pseudomonas aeruginosa interaction with human airway epithelium.PLoS pathogens · 2023Review
- Structural basis for membrane attack complex inhibition by CD59.Nature communications · 2023Article
- Neutralizing the Impact of the Virulence Factor LecA from Pseudomonas aeruginosa on Human Cells with New Glycomimetic Inhibitors.Angewandte Chemie (International ed. in English) · 2023Article
- Manipulation of host cell plasma membranes by intracellular bacterial pathogens.Current opinion in microbiology · 2023Review
- Dimeric Lectin Chimeras as Novel Candidates for Gb3-Mediated Transcytotic Drug Delivery through Cellular Barriers.Pharmaceutics · 2023Article
- A bispecific, crosslinking lectibody activates cytotoxic T cells and induces cancer cell death.Journal of translational medicine · 2022Article
- Novel lectin-based chimeric antigen receptors target Gb3-positive tumour cells.Cellular and molecular life sciences : CMLS · 2022Article
- 100 Hz ROCS microscopy correlated with fluorescence reveals cellular dynamics on different spatiotemporal scales.Nature communications · 2022Article
- Multiplicity of Glycosphingolipid-Enriched Microdomain-Driven Immune Signaling.International journal of molecular sciences · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 3 institutions in 3 countries.
Funding
Abstract
The opportunistic pathogen Pseudomonas aeruginosa has gained precedence over the years due to its ability to develop resistance to existing antibiotics, thereby necessitating alternative strategies to understand and combat the bacterium. Our previous work identified the interaction between the bacterial lectin LecA and its host cell glycosphingolipid receptor globotriaosylceramide (Gb3) as a crucial step for the engulfment of P. aeruginosa via the lipid zipper mechanism. In this study, we define the LecA-associated host cell membrane domain by pull-down and mass spectrometry analysis. We unraveled a predilection of LecA for binding to saturated, long fatty acyl chain-containing Gb3 species in the extracellular membrane leaflet and an induction of dynamic phosphatidylinositol (3,4,5)-trisphosphate (PIP
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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.