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TitleThe structure of the teleost Immunoglobulin M core provides insights on polymeric antibody evolution, assembly, and function.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 7583, Year 2023
Publish dateNov 21, 2023
AuthorsMengfan Lyu / Andrey G Malyutin / Beth M Stadtmueller /
PubMed AbstractPolymeric (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 ...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.
External linksNat Commun / PubMed:37989996 / PubMed Central
MethodsEM (single particle)
Resolution2.78 Å
Structure data

40054

8ghz

EMDB-40054, PDB-8ghz:
Cryo-EM structure of fish immunogloblin M-Fc
Method: EM (single particle) / Resolution: 2.78 Å

Source
  • oncorhynchus mykiss (rainbow trout)
KeywordsIMMUNE SYSTEM / Immunoglobulin M / IgM

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