Structure of the human secretory immunoglobulin M core.

Autor:	Kumar N; Department of Structural Biology, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA., Arthur CP; Department of Structural Biology, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA., Ciferri C; Department of Structural Biology, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA., Matsumoto ML; Department of Structural Biology, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA. Electronic address: matsumoto.marissa@gene.com.
Jazyk:	angličtina
Zdroj:	Structure (London, England : 1993) [Structure] 2021 Jun 03; Vol. 29 (6), pp. 564-571.e3. Date of Electronic Publication: 2021 Jan 28.
DOI:	10.1016/j.str.2021.01.002
Abstrakt:	Immunoglobulins (Ig) A and M are the only human antibodies that form oligomers and undergo transcytosis to mucosal secretions via the polymeric Ig receptor (pIgR). When complexed with the J-chain (JC) and the secretory component (SC) of pIgR, secretory IgA and IgM (sIgA and sIgM) play critical roles in host-pathogen defense. Recently, we determined the structure of sIgA-Fc which elucidated the mechanism of polymeric IgA assembly and revealed an extensive binding interface between IgA-Fc, JC, and SC. Despite low sequence identity shared with IgA-Fc, IgM-Fc also undergoes JC-mediated assembly and binds pIgR. Here, we report the structure of sIgM-Fc and carryout a systematic comparison to sIgA-Fc. Our structural analysis reveals a remarkably conserved mechanism of JC-templated oligomerization and SC recognition of both IgM and IgA through a highly conserved network of interactions. These studies reveal the structurally conserved features of sIgM and sIgA required for function in mucosal immunity. Competing Interests: Declaration of interests All authors are employees of Genentech, Inc., a member of the Roche Group, and may hold stock and options. (Copyright © 2021 Elsevier Ltd. All rights reserved.)
Databáze:	MEDLINE
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