ArticleGlycobiology2010
Identification of glycoproteins targeted by Trypanosoma cruzi trans-sialidase, a virulence factor that disturbs lymphocyte glycosylation.
Article in Glycobiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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Who cites it
26 citing papers in PubMed, 40 citations in OpenAlex.
- Beyond the catalysis of Trypanosoma cruzi trans-sialidases: structure, function, post-translational modifications, intrinsically disordered regions and use of CRISPR/Cas9.Archives of microbiology · 2026Review
- Distinct nanoscale membrane organizations of mucins andbioRxiv : the preprint server for biology · 2026Article
- Sialic acid removal by trans-sialidase modulates MMP-2 activity during Trypanosoma cruzi infection.Biochimie · 2021Article
- Mechanisms Associated withLife (Basel, Switzerland) · 2021Review
- A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-Based Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- Parasite-host glycan interactions during Trypanosoma cruzi infection: trans-Sialidase rides the show.Biochimica et biophysica acta. Molecular basis of disease · 2020Review
- Aiming for the Sweet Spot: Glyco-Immune Checkpoints and γδ T Cells in Targeted Immunotherapy.Frontiers in immunology · 2020Review
- Metabolic Labeling of Surface Neo-sialylglyconjugates Catalyzed by Trypanosoma cruzi trans-Sialidase.Methods in molecular biology (Clifton, N.J.) · 2019Article
- The Trypanosoma cruzi Surface, a Nanoscale Patchwork Quilt.Trends in parasitology · 2017Review
- Role of Inactive and ActiveFrontiers in microbiology · 2017Article
- Chagas Disease Diagnostic Applications: Present Knowledge and Future Steps.Advances in parasitology · 2017Review
- Chemical Glycoproteomics.Chemical reviews · 2016Review
- Costimulatory Effects of an Immunodominant Parasite Antigen Paradoxically Prevent Induction of Optimal CD8 T Cell Protective Immunity.PLoS pathogens · 2016Article
- Sialic Acid Glycobiology Unveils Trypanosoma cruzi Trypomastigote Membrane Physiology.PLoS pathogens · 2016Article
- Modulation of Cell Sialoglycophenotype: A Stylish Mechanism Adopted by Trypanosoma cruzi to Ensure Its Persistence in the Infected Host.Frontiers in microbiology · 2016Review
- Role of Trypanosoma cruzi Trans-sialidase on the Escape from Host Immune Surveillance.Frontiers in microbiology · 2016Review
- Production, purification and crystallization of a trans-sialidase from Trypanosoma vivax.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Trypanosoma cruzi trans-sialidase prevents elicitation of Th1 cell response via interleukin 10 and downregulates Th1 effector cells.Infection and immunity · 2015Article
- The role played by alternative splicing in antigenic variability in human endo-parasites.Parasites & vectors · 2014Review
- IL-17-producing B cells combat parasites.Nature immunology · 2013Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
Trypanosoma cruzi, the agent of the American trypanosomiasis or Chagas disease, bypasses its lack of de novo synthesis of sialic acids by expressing a surface-anchored trans-sialidase. This enzyme transfers sialic acid residues from the host's sialylglycoconjugates to the parasite's galactosylglycoconjugates. In addition to carrying out a pivotal role in parasite persistence/replication within the infected mammal, the trans-sialidase is shed into the bloodstream and induces alterations in the host immune system by modifying the sialylation of the immune cells. A major obstacle to understand these events is the difficulty to identify the transferred sialic acid among all those naturally occurring on the cell surface. Here, we report the use of azido-modified unnatural sialic acid to identify those molecules that act as cell surface acceptors of the sialyl residue in the trans-sialidase-catalyzed reaction, which might then be involved in the immune alterations induced. In living parasites, we readily observed the transfer of azido-sialic acid to surface mucins. When evaluating mouse thymocytes and splenocytes as acceptors of the azido-sugar, a complex pattern of efficiently tagged glycoproteins was revealed. In both leukocyte populations, the main proteins labeled were identified as different CD45 isoforms. Disruption of the cell architecture increased the number and the molecular weight distribution of azido-sialic acid tagged proteins. Nevertheless, CD45 remained to be the main acceptor. Mass spectrometry assays allowed us to identify other acceptors, mainly integrins. The findings reported here provide a molecular basis to understand the abnormalities induced in the immune system by the trans-sialidase during T. cruzi infection.
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Registered trials
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