ReviewGlycoconjugate journal2013
Addition of α-O-GlcNAc to threonine residues define the post-translational modification of mucin-like molecules in Trypanosoma cruzi.
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.
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Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- Glycocalyx-Driven Immunomodulation in Trypanosoma cruzi: Structures, Host Responses, Diagnostic and Therapeutic Targeting.Parasite immunology · 2026Review
- Tumor-Suppressive Cross-Linking of Anti-International journal of molecular sciences · 2024Article
- Specific Recognition of β-Galactofuranose-Containing Glycans of Synthetic Neoglycoproteins by Sera of Chronic Chagas Disease Patients.Molecules (Basel, Switzerland) · 2022Article
- Glycomics, Glycoproteomics, and Glycogenomics: An Inter-Taxa Evolutionary Perspective.Molecular & cellular proteomics : MCP · 2021Review
- Ser and Thr acceptor preferences of the GalNAc-Ts vary among isoenzymes to modulate mucin-type O-glycosylation.Glycobiology · 2020Article
- The Glycan Structure ofMolecules (Basel, Switzerland) · 2020Review
- Comparative Proteomics Analysis ofGenes · 2020Article
- Label-free quantitative proteomic analysis of molting-related proteins of Trichinella spiralis intestinal infective larvae.Veterinary research · 2019Article
- Trypanosoma cruzi surface mucins are involved in the attachment to the Triatoma infestans rectal ampoule.PLoS neglected tropical diseases · 2019Article
- Trypanosoma cruzi 13C-labeled O-Glycan standards for mass spectrometry.Glycobiology · 2019Article
- Engineering a single-chain antibody against Trypanosoma cruzi metacyclic trypomastigotes to block cell invasion.PloS one · 2019Article
- Metabolic Labeling of Surface Neo-sialylglyconjugates Catalyzed by Trypanosoma cruzi trans-Sialidase.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Theft and Reception of Host Cell's Sialic Acid: Dynamics ofFrontiers in immunology · 2019Review
- Congenital Transmission ofFrontiers in microbiology · 2019Review
- Implication of Apoptosis for the Pathogenesis ofFrontiers in immunology · 2017Review
- Evasion and Immuno-Endocrine Regulation in Parasite Infection: Two Sides of the Same Coin in Chagas Disease?Frontiers in microbiology · 2016Review
- Expression and prognostic value of GalNAc-T3 in patients with completely resected small (≤2 cm) peripheral lung adenocarcinoma after IASLC/ATS/ERS classification.OncoTargets and therapy · 2015Article
- Immune Evasion Strategies of Trypanosoma cruzi.Journal of immunology research · 2015Review
- Golgi UDP-GlcNAc:polypeptide O-α-N-Acetyl-d-glucosaminyltransferase 2 (TcOGNT2) regulates trypomastigote production and function in Trypanosoma cruzi.Eukaryotic cell · 2014Article
- Extracellular vesicles in parasitic diseases.Journal of extracellular vesicles · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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