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In-depth glycomics and glycoproteomics of trichomonads

Project Leader
Wilson Iain B.H., Project Leader
Duration:
01.01.2022-31.12.2025
Programme:
Einzelprojekte
Type of Research
Basic Research
Project partners
Medical University Vienna, Wien, Austria.
Contact person: Dr. David Leitsch;
Function of the Project Partner: Partner
Staff
BOKU Research Units
Institute of Biochemistry (DCH/BC)
Funded by
Fonds zur Förderung der wissenschaftlichen Forschung (FWF) , Sensengasse 1, 1090 Wien, Austria
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.
Keywords
Glycobiology;
Glycobiology; Glycomics;
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