Proteomics

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Defining the Structural Features of Complement-Active IgM: Surface Ag linker comparison

ABSTRACT: Immunoglobulin mu (IgM) is a class of mammalian antibodies that are critical for the early stages of adaptive immunity and are the most potent activators of the classical complement cascade. While the relationship between IgM and complement has been appreciated for decades, the structural transitions within IgM upon antigen binding that lead to the activation of the C1 complex remain unresolved. Here we examine the complement activation profiles, binding kinetics, and conformational changes in IgM in different antigen-bound states. Only in the complex with a surface-displayed antigen with multiple Fab arms engaged was the IgM fully capable of driving complement activation. The structural changes within IgM upon antigen binding were monitored by Hydrogen/Deuterium Exchange reveal the predominant structural changes within the Fc core domains upon activation. Collectively, this work establishes key structural and functional qualities that define the complement-active form of IgM.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Charles Mundorff  

LAB HEAD: Miklos Guttman

PROVIDER: PXD056670 | Pride | 2025-04-02

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
Byonic_Fusion_MD4_HeavyChain_Peptide_List.csv Csv
Byonic_Fusion_MD4_JChain_Peptide_List.csv Csv
Byonic_Fusion_MD4_LightChain_Peptide_List.csv Csv
MD4_14Mar2021.fasta Fasta
Watson_surface_linker.zip Other
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Publications

Defining the Features of Complement-Active IgM.

Watson Michael J MJ   Mundorff Charlie C CC   Lynch Eric M EM   Kollman Justin M JM   Kearney John F JF   Guttman Miklos M  

Journal of molecular biology 20250326 12

Immunoglobulin M (IgM) is a class of mammalian antibody that is critical for the early stages of adaptive immunity, and is the most potent Ig-activator of the classical complement cascade. While the relationship between IgM and complement has been appreciated for decades, the structural transitions within IgM upon antigen binding that promote the activation of complement component C1 remain unresolved. Here we examine in vitro complement activation, C1 binding kinetics, and conformational change  ...[more]

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