ArticleThe Journal of clinical investigation2009
The neuropathic potential of anti-GM1 autoantibodies is regulated by the local glycolipid environment in mice.
Article in The Journal of clinical investigation, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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.
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.
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Who cites it
39 citing papers in PubMed, 121 citations in OpenAlex.
- Sialylation in the nervous system: Functions and mechanisms.The Journal of biological chemistry · 2026Review
- Gangliosides and Membrane Microdomains.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Large-scale profiling of antibody reactivity to glycolipids in patients with Guillain-Barré syndrome.Brain : a journal of neurology · 2025Observational
- Guillain-Barré syndrome.Nature reviews. Disease primers · 2024Article
- Article
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- Cell density-dependent membrane distribution of ganglioside GM3 in melanoma cells.Cellular and molecular life sciences : CMLS · 2023Article
- Immune-Mediated Neuropathies: Pathophysiology and Management.International journal of molecular sciences · 2023Review
- Review
- Real time imaging of intra-axonal calcium flux in an explant mouse model of axonal Guillain-Barré syndrome.Experimental neurology · 2022Article
- Schwann cell nodal membrane disruption triggers bystander axonal degeneration in a Guillain-Barré syndrome mouse model.The Journal of clinical investigation · 2022Article
- Guillain-Barré syndrome: expanding the concept of molecular mimicry.Trends in immunology · 2022Review
- Complement inhibition prevents glial nodal membrane injury in a GM1 antibody-mediated mouse model.Brain communications · 2022Article
- Graves' disease with anti-GQ1b antibody syndrome: a rare case report.BMC neurology · 2021Article
- Therapeutic Uses of Bacterial Subunit Toxins.Toxins · 2021Review
- Perisynaptic Schwann cells phagocytose nerve terminal debris in a mouse model of Guillain-Barré syndrome.Journal of the peripheral nervous system : JPNS · 2020Article
- Autoimmune Peripheral Neuropathies and Contribution of Antiganglioside/Sulphatide Autoantibody Testing.Mediterranean journal of rheumatology · 2020Review
- The Neuroimmunology of Guillain-Barré Syndrome and the Potential Role of an Aging Immune System.Frontiers in aging neuroscience · 2020Review
- New era of research on cancer-associated glycosphingolipids.Cancer science · 2019Review
- Differential binding patterns of anti-sulfatide antibodies to glial membranes.Journal of neuroimmunology · 2018Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 2 countries.
Funding
Abstract
Anti-GM1 ganglioside autoantibodies are used as diagnostic markers for motor axonal peripheral neuropathies and are believed to be the primary mediators of such diseases. However, their ability to bind and exert pathogenic effects at neuronal membranes is highly inconsistent. Using human and mouse monoclonal anti-GM1 antibodies to probe the GM1-rich motor nerve terminal membrane in mice, we here show that the antigenic oligosaccharide of GM1 in the live plasma membrane is cryptic, hidden on surface domains that become buried for a proportion of anti-GM1 antibodies due to a masking effect of neighboring gangliosides. The cryptic GM1 binding domain was exposed by sialidase treatment that liberated sialic acid from masking gangliosides including GD1a or by disruption of the live membrane by freezing or fixation. This cryptic behavior was also recapitulated in solid-phase immunoassays. These data show that certain anti-GM1 antibodies exert potent complement activation-mediated neuropathogenic effects, including morphological damage at living terminal motor axons, leading to a block of synaptic transmission. This occurred only when GM1 was topologically available for antibody binding, but not when GM1 was cryptic. This revised understanding of the complexities in ganglioside membrane topology provides a mechanistic account for wide variations in the neuropathic potential of anti-GM1 antibodies.
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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.