ArticleNature communications2022
Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 53 citations in OpenAlex.
- Serum IgM crosslinks hepatitis B subviral particles into supramolecular immune complexes.bioRxiv : the preprint server for biology · 2026Article
- Label-Free Profiling of Immunoglobulin Isotypes Using Solid-State Nanopores.Small methods · 2026Article
- Biophysical properties of IgD determine thresholds for self-tolerance and selection into germinal centers.bioRxiv : the preprint server for biology · 2026Article
- Reconstruction of the Flexible IgM Fc Core Using Atomic Force Microscopy Topography and the AFM-Assembly Pipeline.Journal of molecular recognition : JMR · 2026Article
- Electroosmotic Flow-Driven Nanopore Translocation of Large, Conformationally Dynamic Proteins: Overcoming Steric and Electrostatic Barriers.Journal of the American Chemical Society · 2026Article
- Neutralization of SARS-CoV-2 by IgM-14 via engagement of two distinct spike epitopes.PLoS pathogens · 2026Article
- The fc fragment of IgMs binds C1q to activate the first step of the classical complement pathway, while inhibiting complement-dependent cytotoxicity.The FEBS journal · 2026Article
- Structural mechanism of anti-MHC-I antibody blocking of inhibitory NK cell receptors in tumor immunity.Communications biology · 2026Article
- Fc Profiling of Polyclonal IgG, IgA and IgM by Light Chain Capturing Coupled with NanoRP-LC-MS.JACS Au · 2026Article
- Divalent HIV-1 gp120 Immunogen Exhibits Selective Avidity for Broadly Neutralizing Antibody VRC01 Precursors.Vaccines · 2026Article
- Clinical and immunopathological spectrum of immunoglobulin M pemphigoid: a multicenter case series.Journal der Deutschen Dermatologischen Gesellschaft = Journal of the German Society of Dermatology : JDDG · 2025Article
- Intravaginal delivery of mRNA-encoded antibodies with enhanced breadth and potency for SHIV/HIV protection.Nature communications · 2025Article
- Article
- Structural mechanism of anti-MHC-I antibody blocking of inhibitory NK cell receptors in tumor immunity.Research square · 2025Article
- Chimeric Immunoglobulin and human Immunoglobulin M structures provide insights on joining-chain independent assembly and function.bioRxiv : the preprint server for biology · 2025Article
- Defining the Features of Complement-Active IgM.Journal of molecular biology · 2025Article
- Towards a unifying model for B-cell receptor triggering.Nature reviews. Immunology · 2025Review
- Targeting the epidermal growth factor receptor using IgM antibodies: toward next generation cancer immunotherapy.Frontiers in immunology · 2025Article
- Harnessing IgM for solid tumor therapy: biology, engineering advances, and translational challenges.Frontiers in immunology · 2025Review
- Exploring the structural basis and functional immunodynamics of immunoglobulin M in host defense against fungal pathogens.Frontiers in immunology · 2025Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Immunoglobulin M (IgM) is the most ancient of the five isotypes of immunoglobulin (Ig) molecules and serves as the first line of defence against pathogens. Here, we use cryo-EM to image the structure of the human full-length IgM pentamer, revealing antigen binding domains flexibly attached to the asymmetric and rigid core formed by the Cμ4 and Cμ3 constant regions and the J-chain. A hinge is located at the Cμ3/Cμ2 domain interface, allowing Fabs and Cμ2 to pivot as a unit both in-plane and out-of-plane. This motion is different from that observed in IgG and IgA, where the two Fab arms are able to swing independently. A biased orientation of one pair of Fab arms results from asymmetry in the constant domain (Cμ3) at the IgM subunit interacting most extensively with the J-chain. This may influence the multi-valent binding to surface-associated antigens and complement pathway activation. By comparison, the structure of the Fc fragment in the IgM monomer is similar to that of the pentamer, but is more dynamic in the Cμ4 domain.
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