Evidence map›Paper›PMID 23430107›Full record

ReviewGlycoconjugate journal2013

Addition of α-O-GlcNAc to threonine residues define the post-translational modification of mucin-like molecules in Trypanosoma cruzi.

Lucia Mendonça-Previato, Luciana Penha, Tatiana Cortes Garcez, Christopher Jones, Jose Osvaldo Previato

Open access · hybridAbstract readReview
In one paragraph

Review in Glycoconjugate journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Tumor-Suppressive Cross-Linking of Anti-International journal of molecular sciences · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. The Glycan Structure ofMolecules (Basel, Switzerland) · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Congenital Transmission ofFrontiers in microbiology · 2019
    Review
  15. Review
  16. Review
  17. Article
  18. Immune Evasion Strategies of Trypanosoma cruzi.Journal of immunology research · 2015
    Review
  19. Article
  20. Extracellular vesicles in parasitic diseases.Journal of extracellular vesicles · 2014
    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

5 authors at 2 institutions in 2 countries.

Lucia Mendonça-PreviatoLaboratório de Glicobiologia, Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, 21 941 902, Ilha do Fundão, Cidade Universitária, Rio de Janeiro, RJ, Brazil, luciamp@biof.ufrj.br.
Luciana Penha
Tatiana Cortes Garcez
Christopher Jones
Jose Osvaldo Previato
Universidade Federal do Rio de Janeiro · BRNational Institute for Biological Standards and Control · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trypanosoma cruzi, an intracellular protozoan etiologic agent of Chagas disease is covered by a dense coat of mucin-type glycoproteins, which is important to promote the parasite entry and persistence in the mammalian host cells. The O-glycosylation of T. cruzi mucins (Tc-mucins) is initiated by enzymatic addition of α-O-N-acetylglucosamine (GlcNAc) to threonine (Thr) by the UDP-GlcNAc:polypeptide α-N-acetylglucosaminyltransferase (pp-α-GlcNAcT) in the Golgi. The Tc-mucin is characterized by the presence of a high structural diversity of O-linked oligosaccharides found among different parasite strains, comprising two O-glycan Cores. In the Core 1, from strains principally associated with the domestic transmission cycle of Chagas disease, the GlcNAc O-4 is substituted with a β-galactopyranose (βGalp) unit, and in the most complex oligosaccharides the GlcNAc O-6 is further processed by the addition of β1 → 2-linked Galp residues creating a short linear Galp-containing chain. In the Core 2 structures, expressed by strains isolated from T. cruzi sylvatic hosts, the GlcNAc O-4 carries a β-galactofuranose (βGalf) unit and the GlcNAc O-6 can carry a branched Galpβ1 → 3[Galpβ1 → 2]Galpβ1 → 6 motif. The O-glycans carrying nonreducing terminal βGalp are available for sialylation by a surface T. cruzi trans-sialidase activity. Based on structural results, this review summarizes available data on the highly conserved process, which adds the GlcNAc unit in α-linkage to Thr residues the basis of the post-translational modification system in T. cruzi mucins. In addition, a mechanism unique employed by the parasite to transfer exogenous sialic acid residues to Tc-mucins is presented.

Indexed as

Protein Processing, Post-TranslationalAcetylglucosamineGlycosylationMucinsProtozoan ProteinsThreonineTrypanosoma cruziAcetylglucosamineMucinsProtozoan ProteinsThreonine

Identifiers

PMID23430107
PMCPMC3769586
OpenAlexW2022143262

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.