Evidence map›Paper›PMID 21193402›Full record

ArticleThe Journal of biological chemistry2011

Tn glycosylation of the MUC6 protein modulates its immunogenicity and promotes the induction of Th17-biased T cell responses.

Teresa Freire, Richard Lo-Man, Sylvie Bay, Claude Leclerc

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

29 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Multiple roles and mechanisms of MUC6 in cancer (Review).International journal of molecular medicine · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. A roadmap for translational cancer glycoimmunology at single cell resolution.Journal of experimental & clinical cancer research : CR · 2022
    Review
  10. Article
  11. Article
  12. ASGR1 and Its Enigmatic Relative, CLEC10A.International journal of molecular sciences · 2020
    Review
  13. Article
  14. A Biological and Immunological Characterization ofInternational journal of molecular sciences · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Frontiers in immunology · 2017
    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 3 institutions in 1 country.

Teresa FreireFrom the Institut Pasteur, Department of Immunology, Immune Regulation and Vaccinology Unit, 75015 Paris,; INSERM, U1041, Paris,; the Institut Pasteur, Département de Biologie Structurale et Chimie, Unité de Chimie des Biomolécules, 75015 Paris, and; the CNRS, URA 2128, Paris, France.
Richard Lo-ManFrom the Institut Pasteur, Department of Immunology, Immune Regulation and Vaccinology Unit, 75015 Paris,; INSERM, U1041, Paris.
Sylvie Baythe Institut Pasteur, Département de Biologie Structurale et Chimie, Unité de Chimie des Biomolécules, 75015 Paris, and; the CNRS, URA 2128, Paris, France.
Claude LeclercFrom the Institut Pasteur, Department of Immunology, Immune Regulation and Vaccinology Unit, 75015 Paris,; INSERM, U1041, Paris,. Electronic address: claude.leclerc@pasteur.fr.
Centre National de la Recherche Scientifique · FRInserm · FRInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Tn antigen (α-GalNAc-O-Ser/Thr) is one of the most specific human cancer-associated structures. This antigen, together with mucins, the major carriers of O-glycosylated tumor antigens in adenocarcinomas, are being evaluated as anti-cancer immunotherapeutic targets. In particular, the MUC6 protein, which is normally expressed only in gastric tissues, has been detected in intestinal, pulmonary, colorectal, and breast carcinomas. To develop anti-cancer vaccines based on the Tn antigen, we produced MUC6 proteins with different Tn density by using mixtures of recombinant ppGalNAc-T1, -T2, and -T7. The obtained glycoproteins were characterized and analyzed for their immunological properties, as compared with the non-glycosylated MUC6. We show that these various MUC6:Tn glycoproteins were well recognized by both MUC6 and Tn-specific antibodies. However, Tn glycosylation of the MUC6 protein strongly affected their immunogenicity by partially abrogating Th1 cell responses, and promoting IL-17 responses. Moreover, the non-glycosylated MUC6 was more efficiently presented than MUC6:Tn glycoproteins to specific T CD4(+) hybridomas, suggesting that Tn glycosylation may affect MUC6 processing or MHC binding of the processed peptides. In conclusion, our results indicate that Tn glycosylation of the MUC6 protein strongly affects its B and T cell immunogenicity, and might favor immune escape of tumor cells.

Indexed as

AnimalsAntibodies, NeoplasmAntigens, Tumor-Associated, CarbohydrateCancer VaccinesFemaleGlycosylationHumansInterleukin-17MiceMice, Inbred BALB CMucin-6Th17 CellsTh1 CellsTumor EscapeAntibodies, NeoplasmAntigens, Tumor-Associated, CarbohydrateCancer VaccinesInterleukin-17MUC6 protein, humanMucin-6Tn antigen

Identifiers

PMID21193402
PMCPMC3048667
OpenAlexW1994604751

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.