Evidence map›Paper›PMID 19017944›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2008

Targeting the neonatal fc receptor for antigen delivery using engineered fc fragments.

Wentao Mi, Sylvia Wanjie, Su-Tang Lo, Zhuo Gan, Beatrix Pickl-Herk, Raimund J Ober, E Sally Ward

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.2field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 72 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Review
  4. Article
  5. Advanced Biomaterials for Cell-Specific Modulation and Restore of Cancer Immunotherapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Review
  6. Review
  7. Review
  8. Article
  9. The Neonatal Fc Receptor (FcRn): A Misnomer?Frontiers in immunology · 2019
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. The Role of FcRn in Antigen Presentation.Frontiers in immunology · 2014
    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

7 authors at 2 institutions in 1 country.

Wentao MiDepartment of Immunology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9093, USA.
Sylvia Wanjie
Su-Tang Lo
Zhuo Gan
Beatrix Pickl-Herk
Raimund J Ober
E Sally Ward
The University of Texas Southwestern Medical Center · USThe University of Texas at Dallas · US

Funding

MOLECULAR ANALYSIS OF T CELL RECOGNITION IN EAER01AI042949 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI WARD, ELIZABETH SALLY · 1998 to 2007
$1.7M
CSR NIH HHS RG 2411NIAID NIH HHS AI/NS ROI 42949NIAID NIH HHS R01 AI042949
6 · The paper itself

Abstract

The development of approaches for Ag delivery to the appropriate subcellular compartments of APCs and the optimization of Ag persistence are both of central relevance for the induction of protective immunity or tolerance. The expression of the neonatal Fc receptor, FcRn, in APCs and its localization to the endosomal system suggest that it might serve as a target for Ag delivery using engineered Fc fragment-epitope fusions. The impact of FcRn binding characteristics of an Fc fragment on in vivo persistence allows this property to also be modulated. We have therefore generated recombinant Fc (mouse IgG1-derived) fusions containing the N-terminal epitope of myelin basic protein that is associated with experimental autoimmune encephalomyelitis in H-2(u) mice. The Fc fragments have distinct binding properties for FcRn that result in differences in intracellular trafficking and in vivo half-lives, allowing the impact of these characteristics on CD4(+) T cell responses to be evaluated. To dissect the relative roles of FcRn and the "classical" FcgammaRs in Ag delivery, analogous aglycosylated Fc-MBP fusions have been generated. We show that engineered Fc fragments with increased affinities for FcRn at pH 6.0-7.4 are more effective in delivering Ag to FcRn-expressing APCs in vitro relative to their lower affinity counterparts. However, higher affinity of the FcRn-Fc interaction at near neutral pH results in decreased in vivo persistence. The trade-off between improved FcRn targeting efficiency and lower half-life becomes apparent during analyses of T cell proliferative responses in mice, particularly when Fc-MBP fusions with both FcRn and FcgammaR binding activity are used.

Indexed as

AnimalsAntigen-Presenting CellsAntigensCD4-Positive T-LymphocytesCell ProliferationCHO CellsCricetinaeCricetulusEncephalomyelitis, Autoimmune, ExperimentalEpitopesHistocompatibility Antigens Class IHydrogen-Ion ConcentrationImmunoglobulin Fc FragmentsImmunoglobulin GMiceMice, TransgenicAntigensEpitopesFc receptor, neonatalHistocompatibility Antigens Class IImmunoglobulin Fc FragmentsImmunoglobulin GMyelin Basic ProteinReceptors, FcRecombinant Fusion Proteins

Identifiers

PMID19017944
PMCPMC2738423
OpenAlexW2153889378

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.