In-depth Glycomics and Glycoproteomics of Trichomonads
In-depth Glycomics and Glycoproteomics of Trichomonads
Disciplines
Biology (100%)
Keywords
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N/O-Glycomics,
Glycoproteomics,
Mass Spectrometry,
Trichomonads
Trichomonas vaginalis and Tritrichomonas foetus are major single-cell parasites that respectively infect the urogenital tract of human and bovine hosts, causing globally the most common curable sexually transmitted diseases. These infections are often associated with mild symptoms (e.g., debilitating effects, painful urination, bacterial vaginitis, discomfort during intercourse, vaginal or penis itching, discharges and irritations), but more seriously with increased risk of infertility, cancer and adverse pregnancy outcome. Unfortunately, no vaccine is available and drugs have been less efficient due to resistant isolates. Tritrichomonas foetus is also able to infect the gastrointestinal tract of swine and feline hosts with a faecal - oral route of spread characterized by chronic diarrhoea and tissue infections ; this demonstrates an incredible adaptability to various host environments as well as huge veterinarian impact. Therefore, further research is required to understand the host-parasite interactions of the Trichomonadida in order to develop future eradication strategies relevant to human and animal health. Hereby, we presume that binding to host cells depends on parasite surface protein-linked carbohydrate structures known as glycans. In this project, we aim to characterise the N-glycans and O-glycans present on the parasite cell surface at the molecular level emphasizing on the structural identification of rare glycans and associated glycoproteins as well as examining their interactions with immune innate carbohydrate binding proteins of the host. A mix of mass spectrometry and immobilisation of glycans to arrays will be employed. Overall , this project research will elucidate potential mechanisms of carbohydrate-dependent virulence relevant to these widespread parasitic infections of mammals.
- David Leitsch, Medizinische Universität Wien , associated research partner
Research Output
- 1 Citations
- 9 Publications
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2025
Title Roles of efflux pumps and nitroreductases in metronidazole-resistant Trichomonas vaginalis. DOI 10.1007/s00436-025-08463-7 Type Journal Article Author Paunkov A Journal Parasitology research Pages 21 -
2025
Title Glycoproteomic and Single-Protein Glycomic Analyses Reveal Zwitterionic N-Glycans on Natural and Recombinant Proteins Derived From Insect Cells. DOI 10.1016/j.mcpro.2025.100981 Type Journal Article Author Vanbeselaere J Journal Molecular & cellular proteomics : MCP Pages 100981 -
2024
Title Analysis of Caenorhabditis Protein Glycosylation. DOI 10.1007/978-1-0716-3666-4_8 Type Journal Article Author Paschinger K Journal Methods in molecular biology (Clifton, N.J.) Pages 123-138 -
2024
Title Recognition of Highly Branched N-Glycans of the Porcine Whipworm by the Immune System. DOI 10.1016/j.mcpro.2024.100711 Type Journal Article Author Eckmair B Journal Molecular & cellular proteomics : MCP Pages 100711 -
2022
Title Editorial: Characterization, Biosynthesis and Biological Functions of Novel Glyco-Epitopes DOI 10.3389/fmolb.2022.871037 Type Journal Article Author Yan S Journal Frontiers in Molecular Biosciences Pages 871037 Link Publication -
2024
Title Revisiting the isolation and characterisation of Entamoeba histolytica lipopeptidophosphoglycan. DOI 10.1007/s00436-024-08149-6 Type Journal Article Author Nagode A Journal Parasitology research Pages 138 -
2023
Title N-glycan antennal modifications are altered in Caenorhabditis elegans lacking the HEX-4 N-acetylgalactosamine-specific hexosaminidase. DOI 10.1016/j.jbc.2023.103053 Type Journal Article Author Paschinger K Journal The Journal of biological chemistry Pages 103053 Link Publication -
2023
Title Recognition of highly branched N-glycans of the porcine whipworm by the immune system. DOI 10.1101/2023.09.21.557549 Type Journal Article Author Eckmair B Journal bioRxiv : the preprint server for biology -
2023
Title Molecular characterisation of Entamoeba histolytica UDP-glucose 4-epimerase, an enzyme able to provide building blocks for cyst wall formation. DOI 10.1371/journal.pntd.0011574 Type Journal Article Author Nagode A Journal PLoS neglected tropical diseases