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TitleCD5L associates with IgM via the J chain.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 8397, Year 2024
Publish dateSep 27, 2024
AuthorsYuxin Wang / Chen Su / Chenggong Ji / Junyu Xiao /
PubMed AbstractCD5 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 ...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 Ca-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.
External linksNat Commun / PubMed:39333069 / PubMed Central
MethodsEM (single particle)
Resolution3.39 - 3.41 Å
Structure data

37936

8wyr

EMDB-37936, PDB-8wyr:
Cryo-EM structure of human CD5L bound to IgM-Fc/J
Method: EM (single particle) / Resolution: 3.39 Å

37937

8wys

EMDB-37937, PDB-8wys:
Local map of human CD5L bound to IgM-Fc/J
Method: EM (single particle) / Resolution: 3.41 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / immunoglobulin / CD5 antigen-like / pentamer

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