Evidence map›Paper›PMID 21502329›Full record

ArticleThe Journal of experimental medicine2011

MHCII glycosylation modulates Bacteroides fragilis carbohydrate antigen presentation.

Sean O Ryan, Jason A Bonomo, Fan Zhao, Brian A Cobb

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Article
  3. Immunometabolism (Cobham, Surrey) · 2023
    Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. The Role of Glycosylation in Inflammatory Diseases.Advances in experimental medicine and biology · 2021
    Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 1 country.

Sean O RyanDepartment of Pathology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Jason A Bonomo
Fan Zhao
Brian A Cobb
Case Western Reserve University · USUniversity School · US

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI ORR, SALLY L · 2001 to 2010
$80.3M
Antigenic Carbohydrate Structure, Function, and SpecificityR01GM082916 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI COBB, BRIAN A · 2009 to 2016
$1.9M
T cell Dependent Immune Responses to Carbohydrate AntigensDP2OD004225 · OD · CASE WESTERN RESERVE UNIVERSITY · PI COBB, BRIAN A · 2008 to 2008
$1.9M
NIGMS NIH HHS GM062116NIGMS NIH HHS GM082916NIGMS NIH HHS R01 GM082916NIGMS NIH HHS U54 GM062116NIH HHS DP2 OD004225NIH HHS OD004225
6 · The paper itself

Abstract

N-linked glycans are thought to protect class II major histocompatibility complex (MHC) molecules (MHCII) from proteolytic cleavage and assist in arranging proteins within the immune synapse, but were not thought to directly participate in antigen presentation. Here, we report that antigen-presenting cells (APCs) lacking native complex N-glycans showed reduced MHCII binding and presentation of the T cell activating glycoantigen (GlyAg) polysaccharide A from Bacteroides fragilis but not conventional peptides. APCs lacking native N-glycans also failed to mediate GlyAg-driven T cell activation but activated T cells normally with protein antigen. Mice treated with the mannosidase inhibitor kifunensine to prevent the formation of complex N-glycans were unable to expand GlyAg-specific T cells in vivo upon immunization, yet adoptive transfer of normally glycosylated APCs into these animals overcame this defect. Our findings reveal that MHCII N-glycosylation directly impacts binding and presentation of at least one class of T cell-dependent antigen.

Indexed as

AlkaloidsAnimalsAntigen PresentationAntigen-Presenting CellsAntigens, BacterialBacteroides fragilisGlycosylationHEK293 CellsHistocompatibility Antigens Class IIHumansLymphocyte ActivationMannosidasesMicePolysaccharides, BacterialT-LymphocytesAlkaloidsAntigens, BacterialHistocompatibility Antigens Class IIkifunensineMannosidasesPolysaccharides, Bacterial

Identifiers

PMID21502329
PMCPMC3092352
OpenAlexW2138727782

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.