Structure of the human secretory immunoglobulin M core

被引：30
作者：
Kumar, Nikit [1 ,2 ]
Arthur, Christopher P. [1 ]
Ciferri, Claudio [1 ]
Matsumoto, Marissa L. [1 ]
机构：
[1] Genentech Inc, Dept Struct Biol, 1 DNA Way, San Francisco, CA 94080 USA
[2] Janssen Res & Dev, Dept Struct & Prot Sci, 200 McKean Rd, Spring House, PA 19477 USA
来源：
STRUCTURE | 2021年 / 29卷 / 06期
关键词：
CRYO-EM; IGM; RECEPTOR; POLYMERIZATION; VISUALIZATION; VALIDATION; BINDING; TOOLS; CHAIN;
D O I：
10.1016/j.str.2021.01.002
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Immunoglobulins (Ig) A and Mare 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.
引用
收藏
页码：564 / +
页数：11
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