CD5L associates with IgM via the J chain

Yuxin Wang, Chen Su, Chenggong Ji and Junyu Xiao ()
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Yuxin Wang: Peking University
Chen Su: Peking University
Chenggong Ji: Peking University
Junyu Xiao: Peking University

Nature Communications, 2024, vol. 15, issue 1, 1-10

Abstract: Abstract CD5 antigen-like (CD5L), also known as Spα or AIM (Apoptosis inhibitor of macrophage), emerges as an integral component of serum immunoglobulin M (IgM). However, the molecular mechanism underlying the interaction between IgM and CD5L has remained elusive. In this study, we present a cryo-electron microscopy structure of the human IgM pentamer core in complex with CD5L. Our findings reveal that CD5L binds to the joining chain (J chain) in a Ca2+-dependent manner and further links to IgM via a disulfide bond. We further corroborate recently published data that CD5L reduces IgM binding to the mucosal transport receptor pIgR, but does not impact the binding of the IgM-specific receptor FcμR. Additionally, CD5L does not interfere with IgM-mediated complement activation. These results offer a more comprehensive understanding of IgM and shed light on the function of the J chain in the immune system.

Date: 2024
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DOI: 10.1038/s41467-024-52175-y

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