EMD-20750

Single-particle
3.0 Å
EMD-20750 Deposition: 20/09/2019
Map released: 19/02/2020
Last modified: 09/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-20750

Structure of tetrameric sIgA complex (Class 1)

EMD-20750

Single-particle
3.0 Å
EMD-20750 Deposition: 20/09/2019
Map released: 19/02/2020
Last modified: 09/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: tetrameric sIgA complex (Class 1)
Fitted models: 6ue8 (Avg. Q-score: 0.4)

Deposition Authors: Kumar N , Arthur CP
Structure of the secretory immunoglobulin A core.
Kumar N , Arthur CP , Ciferri C , Matsumoto ML
(2020) Science , 367 , 1008 - 1014
PUBMED: 32029686
DOI: doi:10.1126/science.aaz5807
ISSN: 1095-9203
ASTM: SCIEAS
Abstract:
Secretory immunoglobulin A (sIgA) represents the immune system's first line of defense against mucosal pathogens. IgAs are transported across the epithelium, as dimers and higher-order polymers, by the polymeric immunoglobulin receptor (pIgR). Upon reaching the luminal side, sIgAs mediate host protection and pathogen neutralization. In recent years, an increasing amount of attention has been given to IgA as a novel therapeutic antibody. However, despite extensive studies, sIgA structures have remained elusive. Here, we determine the atomic resolution structures of dimeric, tetrameric, and pentameric IgA-Fc linked by the joining chain (JC) and in complex with the secretory component of the pIgR. We suggest a mechanism in which the JC templates IgA oligomerization and imparts asymmetry for pIgR binding and transcytosis. This framework will inform the design of future IgA-based therapeutics.