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-Structure paper
| Title | Structural insights into secretory immunoglobulin A and its interaction with a pneumococcal adhesin. |
|---|---|
| Journal, issue, pages | Cell Res, Vol. 30, Issue 7, Page 602-609, Year 2020 |
| Publish date | May 12, 2020 |
Authors | Yuxin Wang / Guopeng Wang / Yaxin Li / Qinyu Zhu / Hao Shen / Ning Gao / Junyu Xiao / ![]() |
| PubMed Abstract | Secretory Immunoglobulin A (SIgA) is the most abundant antibody at the mucosal surface. It possesses two additional subunits besides IgA: the joining chain (J-chain) and secretory component (SC). SC ...Secretory Immunoglobulin A (SIgA) is the most abundant antibody at the mucosal surface. It possesses two additional subunits besides IgA: the joining chain (J-chain) and secretory component (SC). SC is the ectodomain of the polymeric immunoglobulin receptor (pIgR), which functions to transport IgA to the mucosa. How the J-chain and pIgR/SC facilitate the assembly and secretion of SIgA remains incompletely understood. Furthermore, during the infection of Streptococcus pneumoniae, the pneumococcal adhesin SpsA hijacks pIgR/SC and SIgA to gain entry to human cells and evade host defense. How SpsA targets pIgR/SC and SIgA also remains elusive. Here we report a cryo-electron microscopy structure of the Fc region of IgA1 (Fcα) in complex with the J-chain and SC (Fcα-J-SC), which reveals the organization principle of SIgA. We also present a structure of Fcα-J-SC complexed with SpsA, which uncovers the specific interactions between SpsA and human pIgR/SC. These results advance the molecular understanding of SIgA and shed light on S. pneumoniae pathogenesis. |
External links | Cell Res / PubMed:32398862 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.15 - 3.27 Å |
| Structure data | EMDB-30004, PDB-6lx3: EMDB-30008, PDB-6lxw: |
| Source |
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Keywords | IMMUNE SYSTEM / immunoglobulin / dimer / transcytosis / secreted |
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homo sapiens (human)
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