Evidence map›Paper›PMID 32398862›Full record

ArticleCell research2020

Structural insights into secretory immunoglobulin A and its interaction with a pneumococcal adhesin.

Yuxin Wang, Guopeng Wang, Yaxin Li, Qinyu Zhu, Hao Shen, Ning Gao, Junyu Xiao

Open access · bronzeAbstract read
In one paragraph

Article in Cell research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.6field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Structural promiscuity in the human circulatory IgA1 clonal repertoire.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Science advances · 2025
    Article
  7. Review
  8. Article
  9. CD5L associates with IgM via the J chain.Nature communications · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Structural basis for Fc receptor recognition of immunoglobulin M.Nature structural & molecular biology · 2023
    Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Yuxin Wang *State Key Laboratory of Protein and Plant Gene Research, Peking University, Beijing, 100871, China.ORCID http://orcid.org/0000-0002-4490-3995
Guopeng Wang *School of Life Sciences, Peking University, Beijing, 100871, China.
Yaxin Li *State Key Laboratory of Protein and Plant Gene Research, Peking University, Beijing, 100871, China.
Qinyu ZhuState Key Laboratory of Protein and Plant Gene Research, Peking University, Beijing, 100871, China.
Hao ShenState Key Laboratory of Protein and Plant Gene Research, Peking University, Beijing, 100871, China.
Ning GaoSchool of Life Sciences, Peking University, Beijing, 100871, China.ORCID http://orcid.org/0000-0003-3067-9993
Junyu XiaoState Key Laboratory of Protein and Plant Gene Research, Peking University, Beijing, 100871, China. junyuxiao@pku.edu.cn.ORCID http://orcid.org/0000-0003-1822-1701
Peking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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 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.

Indexed as

Adhesins, BacterialBacterial ProteinsCryoelectron MicroscopyHumansImmunoglobulin A, SecretoryModels, MolecularProtein BindingProtein DomainsProtein MultimerizationAdhesins, BacterialBacterial ProteinsImmunoglobulin A, SecretorySpsA protein, Streptococcus pneumoniae

Identifiers

PMID32398862
PMCPMC7343866
OpenAlexW3025038177

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.