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The structure of the teleost Immunoglobulin M core provides insights on polymeric antibody evolution, assembly, and function

Author

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  • Mengfan Lyu

    (University of Illinois Urbana-Champaign)

  • Andrey G. Malyutin

    (California Institute of Technology
    Beckman Institute, California Institute of Technology
    Takeda Pharmaceuticals)

  • Beth M. Stadtmueller

    (University of Illinois Urbana-Champaign
    University of Illinois Urbana-Champaign
    University of Illinois Urbana-Champaign
    University of Illinois Urbana-Champaign)

Abstract

Polymeric (p) immunoglobulins (Igs) serve broad functions during vertebrate immune responses. Typically, pIgs contain between two and six Ig monomers, each with two antigen binding fragments and one fragment crystallization (Fc). In addition, many pIgs assemble with a joining-chain (JC); however, the number of monomers and potential to include JC vary with species and heavy chain class. Here, we report the cryo-electron microscopy structure of IgM from a teleost (t) species, which does not encode JC. The structure reveals four tIgM Fcs linked through eight C-terminal tailpieces (Tps), which adopt a single β-sandwich-like domain (Tp assembly) located between two Fcs. Specifically, two of eight heavy chains fold uniquely, resulting in a structure distinct from mammalian IgM, which typically contains five IgM monomers, one JC and a centrally-located Tp assembly. Together with mutational analysis, structural data indicate that pIgs have evolved a range of assembly mechanisms and structures, each likely to support unique antibody effector functions.

Suggested Citation

  • Mengfan Lyu & Andrey G. Malyutin & Beth M. Stadtmueller, 2023. "The structure of the teleost Immunoglobulin M core provides insights on polymeric antibody evolution, assembly, and function," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43240-z
    DOI: 10.1038/s41467-023-43240-z
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    References listed on IDEAS

    as
    1. Qu Chen & Rajesh Menon & Lesley J. Calder & Pavel Tolar & Peter B. Rosenthal, 2022. "Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Chris T. Amemiya & Jessica Alföldi & Alison P. Lee & Shaohua Fan & Hervé Philippe & Iain MacCallum & Ingo Braasch & Tereza Manousaki & Igor Schneider & Nicolas Rohner & Chris Organ & Domitille Chalopi, 2013. "The African coelacanth genome provides insights into tetrapod evolution," Nature, Nature, vol. 496(7445), pages 311-316, April.
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