Evidence map›Paper›PMID 33107820›Full record

ArticleeLife2020

The structures of secretory and dimeric immunoglobulin A.

Sonya Kumar Bharathkar, Benjamin W Parker, Andrey G Malyutin, Nandan Haloi, Kathryn E Huey-Tubman, Emad Tajkhorshid, Beth M Stadtmueller

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 69 citations in OpenAlex.

  1. Trial
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  10. Science advances · 2025
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  19. Mini-review: Serum immunoglobulins and MASLD.Frontiers in immunology · 2025
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Sonya Kumar Bharathkar *Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, United States.ORCID 0000-0002-3637-4990
Benjamin W Parker *Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, United States.ORCID 0000-0002-1464-1189
Andrey G MalyutinDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Nandan HaloiCenter for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, United States.
Kathryn E Huey-TubmanDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Emad TajkhorshidDepartment of Biochemistry, University of Illinois Urbana-Champaign, Urbana, United States.ORCID 0000-0001-8434-1010
Beth M StadtmuellerDepartment of Biochemistry, University of Illinois Urbana-Champaign, Urbana, United States.ORCID 0000-0003-0637-3206
University of Illinois Urbana-Champaign · USCalifornia Institute of Technology · US

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
NEONATAL FC RECEPTOR/IGG INTERACTIONR01AI041239 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI BJORKMAN, PAMELA J · 1997 to 2018
$2.3M
National Institute of Allergy and Infectious Diseases AI04123NIAID NIH HHS R01 AI041239NIGMS NIH HHS P41 GM103311NIGMS NIH HHS P41 GM10460NIGMS NIH HHS R01 GM129325
6 · The paper itself

Abstract

Secretory (S) Immunoglobulin (Ig) A is the predominant mucosal antibody, which binds pathogens and commensal microbes. SIgA is a polymeric antibody, typically containing two copies of IgA that assemble with one joining-chain (JC) to form dimeric (d) IgA that is bound by the polymeric Ig-receptor ectodomain, called secretory component (SC). Here, we report the cryo-electron microscopy structures of murine SIgA and dIgA. Structures reveal two IgAs conjoined through four heavy-chain tailpieces and the JC that together form a β-sandwich-like fold. The two IgAs are bent and tilted with respect to each other, forming distinct concave and convex surfaces. In SIgA, SC is bound to one face, asymmetrically contacting both IgAs and JC. The bent and tilted arrangement of complex components limits the possible positions of both sets of antigen-binding fragments (Fabs) and preserves steric accessibility to receptor-binding sites, likely influencing antigen binding and effector functions.

Indexed as

AnimalsCell LineCryoelectron MicroscopyHumansImmunoglobulin AImmunoglobulin A, SecretoryMiceModels, MolecularProtein ConformationSecretory ComponentImmunoglobulin AImmunoglobulin A, SecretorySecretory Componentantibodycryo electron microscopyimmunologyinflammationmolecular biophysicsmousesecretory immunoglobulinstructural biology

Identifiers

PMID33107820
PMCPMC7707832
OpenAlexW3093770047

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.