Evidence map›Paper›PMID 18256279›Full record

ArticleMolecular biology of the cell2008

The chicken yolk sac IgY receptor, a mammalian mannose receptor family member, transcytoses IgY across polarized epithelial cells.

Devin B Tesar, Evelyn J Cheung, Pamela J Bjorkman

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. IgYs: on her majesty's secret service.Frontiers in immunology · 2023
    Review
  4. Structure of PLA2R reveals presentation of the dominant membranous nephropathy epitope and an immunogenic patch.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. The Neonatal Fc Receptor (FcRn): A Misnomer?Frontiers in immunology · 2019
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Membranous nephropathy: from models to man.The Journal of clinical investigation · 2014
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Avian IgY antibodies and their recombinant equivalents in research, diagnostics and therapy.Biologicals : journal of the International Association of Biological Standardization · 2012
    Review
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

3 authors at 1 institution in 1 country.

Devin B TesarDivision of Biology and Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
Evelyn J Cheung
Pamela J Bjorkman
California Institute of Technology · US

Funding

Analysis of the Neonatal Fc Receptor/IgG InteractionR37AI041239 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI BJORKMAN, PAMELA J · 2004 to 2013
$3.7M
NIAID NIH HHS 2 R37 AI041239-06A1NIAID NIH HHS R37 AI041239
6 · The paper itself

Abstract

In mammals the transfer of passive immunity from mother to young is mediated by the MHC-related receptor FcRn, which transports maternal IgG across epithelial cell barriers. In birds, maternal IgY in egg yolk is transferred across the yolk sac to passively immunize chicks during gestation and early independent life. The chicken yolk sac IgY receptor (FcRY) is the ortholog of the mammalian phospholipase A2 receptor, a mannose receptor family member, rather than an FcRn or MHC homolog. FcRn and FcRY both exhibit ligand binding at the acidic pH of endosomes and ligand release at the slightly basic pH of blood. Here we show that FcRY expressed in polarized mammalian epithelial cells functioned in endocytosis, bidirectional transcytosis, and recycling of chicken FcY/IgY. Confocal immunofluorescence studies demonstrated that IgY binding and endocytosis occurred at acidic but not basic pH, mimicking pH-dependent uptake of IgG by FcRn. Colocalization studies showed FcRY-mediated internalization via clathrin-coated pits and transport involving early and recycling endosomes. Disruption of microtubules partially inhibited apical-to-basolateral and basolateral-to-apical transcytosis, but not recycling, suggesting the use of different trafficking machinery. Our results represent the first cell biological evidence of functional equivalence between FcRY and FcRn and provide an intriguing example of how evolution can give rise to systems in which similar biological requirements in different species are satisfied utilizing distinct protein folds.

Indexed as

AnimalsCell LineCell PolarityChick EmbryoEndocytosisEpithelial CellsFemaleHistocompatibility Antigens Class IImmunization, PassiveImmunoglobulinsKidney Tubules, CollectingLectins, C-TypeMannose-Binding LectinsMannose ReceptorRatsReceptors, Cell SurfaceFc receptor, neonatalHistocompatibility Antigens Class IIgYImmunoglobulinsLectins, C-TypeMannose-Binding LectinsMannose ReceptorReceptors, Cell SurfaceReceptors, FcReceptors, Phospholipase A2Recombinant Proteins

Identifiers

PMID18256279
PMCPMC2291411
OpenAlexW2116365541

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.