Evidence map›Paper›PMID 21159783›Full record

ArticleGlycobiology2011

The binding specificity of the marker antibodies Tra-1-60 and Tra-1-81 reveals a novel pluripotency-associated type 1 lactosamine epitope.

Suvi Natunen, Tero Satomaa, Virve Pitkänen, Hanna Salo, Milla Mikkola, Jari Natunen, Timo Otonkoski, Leena Valmu

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

53 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Glycan Markers of Pluripotent Stem Cells.Advances in experimental medicine and biology · 2026
    Review
  3. Review
  4. Review
  5. Glycosylation in Stem Cell Biology.Handbook of experimental pharmacology · 2025
    Review
  6. Germ cell tumors, cell surface markers, and the early search for human pluripotent stem cells.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Paradoxical Expression of R-10G-reactive Antigen in Human Testicular Embryonal Carcinoma.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. B3GALT5 knockout alters gycosphingolipid profile and facilitates transition to human naïve pluripotency.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. The sTRA Plasma Biomarker: Blinded Validation of Improved Accuracy Over CA19-9 in Pancreatic Cancer Diagnosis.Clinical cancer research : an official journal of the American Association for Cancer Research · 2019
    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

8 authors at 3 institutions in 1 country.

Suvi NatunenFinnish Red Cross Blood Service, Kivihaantie 7, 00310 Helsinki, Finland.
Tero Satomaa
Virve Pitkänen
Hanna Salo
Milla Mikkola
Jari Natunen
Timo Otonkoski
Leena Valmu
Finnish Red Cross · FIGlykos (Finland) · FIUniversity of Helsinki · FI

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI PAULSON, JAMES C · 2001 to 2010
$80.3M
NIGMS NIH HHS GM62116
6 · The paper itself

Abstract

The expression of the epitopes recognized by the monoclonal antibodies Tra-1-60 and Tra-1-81 is routinely used to assess the pluripotency status of human embryonic stem cells (hESCs) and induced pluripotent stem (iPS) cells. Although it is known that the epitopes recognized by Tra-1-60 and Tra-1-81 are carbohydrates, the exact molecular identity of these epitopes has been unclear. Glycan array analysis with more than 500 oligosaccharide structures revealed specific binding of Tra-1-60 and Tra-1-81 to two molecules containing terminal type 1 lactosamine: Galβ1-3GlcNAcβ1-3Galβ1-4GlcNAc and Galβ1-3GlcNAcβ1-3Galβ1-4GlcNAcβ1-6(Galβ1-3GlcNAcβ1-3)Galβ1-4Glc. The type 1 disaccharide in itself was not sufficient for binding, indicating that the complete epitope requires an extended tetrasaccharide structure where the type 1 disaccharide is β1,3-linked to type 2 lactosamine. Our mass spectrometric analysis complemented with glycosidase digestions of hESC O-glycans indicated the presence of the extended tetrasaccharide epitope on an O-glycan with the likely structure Galβ1-3GlcNAcβ1-3Galβ1-4GlcNAcβ1-6(Galβ1-3)GalNAc. Thus, the present data indicate that the pluripotency marker antibodies Tra-1-60 and Tra-1-81 recognize the minimal epitope Galβ1-3GlcNAcβ1-3Galβ1-4GlcNAc, which is present in hESCs as a part of a mucin-type O-glycan structure. The exact molecular identity of Tra-1-60 and Tra-1-81 is important for the development of improved tools to characterize the pluripotent phenotype.

Indexed as

Amino SugarsEpitopesAntibodiesAntibody SpecificityBinding SitesBiomarkersCarbohydrate ConformationCarbohydrate SequenceEmbryonic Stem CellsFlow CytometryGlycoside HydrolasesHumansMass SpectrometryMolecular Sequence DataOligosaccharidesPluripotent Stem CellsAmino SugarsAntibodiesBiomarkersEpitopesGlycoside HydrolaseslactosamineOligosaccharides

Identifiers

PMID21159783
PMCPMC3150112
OpenAlexW2129665916

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.