In-depth glycomics and glycoproteomics of trichomonads
Abstract
Wider Research Context: Trichomonas vaginalis and Tritrichomonas foetus are protist parasites which commonly infect the urogenital or digestive tracts of mammalian hosts leading to mild symptoms and increased risks of infertility, cancer, viral infection and adverse pregnancy outcome. Unfortunately, no vaccine is available and drugs have been less efficient since the emergence of resistant isolates in 1962. Therefore, further research is required to understand the host-parasite interactions of the Trichomonadida order to develop future eradication strategies relevant to human and animal health. Hypotheses: It is hypothesized that there are differences in protein glycosylation and glycoproteome of T. vaginalis and T. foetus isolates that correlates with their genotype or host of origin while N/O-glycans of these species are recognized by carbohydrate binding proteins of the host innate immune system. Methods: This glycomic project will define the protein glycosylation of T. vaginalis and T. foetus through the fine structural characterisation of their N/O-glycans from several reference and clinical isolates. The parasitic glycans will be release by enzymatic and chemical treatments prior to be fluorescently labelled and characterised by two-dimensions HPLC and MALDI-ToF. The parasitic N/O-glycans will be immobilised via glycan-array to investigate their recognition by relevant host innate immunity carbohydrate binding proteins. The parasitic glycoproteomics will aim to enriched and identify specific glycoproteomes based on rare glyco-epitopes via lectin affinity chromatography and LC-MS. Innovation: This in-depth structural mapping of N/O-glycans from T. vaginalis and T. foetus will define trichomonad protein glycosylation and therefore the glycosylation evolution of eukaryote protist parasites. This large glycomic investigation will highlight differences between trichomonad isolates in terms of genotype and host of origin. This first trichomonad-based glycan-array will reveal the parasitic N/O-glycan interactions with host innate immune carbohydrate binding proteins. The glycoproteomics will unveil glycoprotein backbones and their N/O-linked glycans to identify potentially highly immunogenic glycoproteins.
- Glycomics
- Glycobiology
Publications
N-glycan antennal modifications are altered in Caenorhabditis elegans lacking the HEX-4 N-acetylgalactosamine-specific hexosaminidase.
Autoren: Paschinger, K; Wöls, F; Yan, S; Jin, C; Vanbeselaere, J; Dutkiewicz, Z; Arcalis, E; Malzl, D; Wilson, IBH; Jahr: 2023
Journal articles
Project staff
Jorick Vanbeselaere
Dr. Jorick Vanbeselaere
jorick.vanbeselaere@boku.ac.at
Project Leader
07.02.2022 - 31.12.2025
Iain B.H. Wilson
ao.Univ.Prof. Dr.phil. Iain B.H. Wilson
iain.wilson@boku.ac.at
Tel: +43 1 47654-77216, 77217
Project Leader
01.01.2022 - 06.02.2022
BOKU partners
External partners
Medical University Vienna
Dr. David Leitsch
partner