Expert Lecture Details IgM and IgA Assembly, Complement Activation and FcRL5 Structure
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An ImmuneZoom expert lecture, published on the Immune Zoom YouTube channel on October 15, 2026, covered the structural biology of antibody assembly and effector function. The speaker explained how the J chain and the IgM tailpiece drive pentamer formation and engage the polymeric Ig receptor for mucosal transport, and how stable binding of CD5L at the pentamer gap blocks that transport while leaving complement activation and FcμR binding intact. Engineering work was also presented: shortening the human IgM tailpiece to 11-16 residues or substituting the Xenopus IgX tailpiece produces efficient hexamers with stronger C1q recruitment. Additional topics included FcRL5, an IgG Fc receptor that binds two adjacent IgG Fc regions at 1:2 stoichiometry and drives lysosomal internalization, and engineered hexameric IgG targeting CD20 with enhanced complement-dependent cytotoxicity in vitro.
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- youtube.comExpert Lecture Details IgM and IgA Assembly, Complement Activation and FcRL5 Receptor Structure
An ImmuneZoom expert lecture on the Immune Zoom YouTube channel covered the structural biology of IgM and IgA assembly, secretion and complement activation. Key points include how the J chain and IgM tailpiece drive pentamer formation and interact with the polymeric Ig receptor for mucosal transport, how the stable binding of CD5L at the pentamer gap blocks that transport without affecting complement activation or FcμR binding, and how shortening the human IgM tailpiece to 11–16 residues or substituting the Xenopus IgX tailpiece yields efficient hexamers with stronger C1q recruitment. The lecture also described FcRL5 as an IgG Fc receptor that binds two adjacent IgG Fc regions at 1:2 stoichiometry and mediates lysosomal internalization, plus engineered hexameric IgG targeting CD20 showing enhanced complement-dependent cytotoxicity in vitro.
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