Evidence map›Paper›PMID 27412418›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2016

Biophysical and Biochemical Characterization of Avian Secretory Component Provides Structural Insights into the Evolution of the Polymeric Ig Receptor.

Beth M Stadtmueller, Zhongyu Yang, Kathryn E Huey-Tubman, Helena Roberts-Mataric, Wayne L Hubbell, Pamela J Bjorkman

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

7 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Role of Polymeric Immunoglobulin Receptor in IgA and IgM Transcytosis.International journal of molecular sciences · 2021
    Review
  5. Article
  6. The contribution of modern EPR to structural biology.Emerging topics in life sciences · 2018
    Article
  7. Article
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

6 authors at 3 institutions in 1 country.

Beth M StadtmuellerDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125;ORCID 0000-0003-0637-3206
Zhongyu YangDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095; and Jules Stein Eye Institute, University of California, Los Angeles, Los Angeles, CA 90095.ORCID 0000-0002-3018-3608
Kathryn E Huey-TubmanDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125;ORCID 0000-0002-4683-8138
Helena Roberts-MataricDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125;
Wayne L HubbellDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095; and Jules Stein Eye Institute, University of California, Los Angeles, Los Angeles, CA 90095.
Pamela J BjorkmanDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125; bjorkman@caltech.edu.ORCID 0000-0002-2277-3990
California Institute of Technology · USPasadena City College · USUniversity of California, Los Angeles · US

Funding

Vision Research Core at UCLAP30EY000331 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Xian-Jie Yang · 1985 to 2026
$16.8M
MOLECULAR BASIS OF MEMBRANE EXCITATIONR01EY005216 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUBBELL, WAYNE L · 1985 to 2019
$9.8M
NEONATAL FC RECEPTOR/IGG INTERACTIONR01AI041239 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI BJORKMAN, PAMELA J · 1997 to 2018
$2.3M
MOLECULAR BASIS OF MEMBRANE EXCITATIONR37EY005216 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUBBELL, WAYNE L · 1990 to 1999
–
NEI NIH HHS P30 EY000331NEI NIH HHS R01 EY005216NEI NIH HHS R37 EY005216NIAID NIH HHS R01 AI041239
6 · The paper itself

Abstract

The polymeric Ig receptor (pIgR) transports polymeric Abs across epithelia to the mucosa, where proteolytic cleavage releases the ectodomain (secretory component [SC]) as an integral component of secretory Abs, or as an unliganded protein that can mediate interactions with bacteria. SC is conserved among vertebrates, but domain organization is variable: mammalian SC has five domains (D1-D5), whereas avian, amphibian, and reptilian SC lack the D2 domain, and fish SC lacks domains D2-D4. In this study, we used double electron-electron resonance spectroscopy and surface plasmon resonance binding studies to characterize the structure, dynamics, and ligand binding properties of avian SC, avian SC domain variants, and a human SC (hSC) variant lacking the D2 domain. These experiments demonstrated that, unlike hSC, which adopts a compact or "closed" domain arrangement, unliganded avian SC is flexible and exists in both closed and open states, suggesting that the mammalian SC D2 domain stabilizes the closed conformation observed for hSC D1-D5. Experiments also demonstrated that avian and mammalian pIgR share related, but distinct, mechanisms of ligand binding. Together, our data reveal differences in the molecular recognition mechanisms associated with evolutionary changes in the pIgR protein.

Indexed as

ChickensEvolution, MolecularAmino Acid SequenceAnimalsBase SequenceChromatography, GelHumansProtein DomainsReceptors, Polymeric ImmunoglobulinSecretory ComponentSequence AlignmentSurface Plasmon ResonanceReceptors, Polymeric ImmunoglobulinSecretory Component

Identifiers

PMID27412418
PMCPMC4976031
OpenAlexW2468337421

What OpenQuestion holds

Textmetadata
LicenceTDM
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.