N-Glycoproteomics of the Apicomplexan Parasite Toxoplasma gondii.
Ontology highlight
ABSTRACT: Protein N-glycosylation influences protein folding, stability, and trafficking, and has prominent functions in cell-cell adhesion and recognition. For the parasite Toxoplasma gondii, N-glycosylation of proteins is crucial for initial adhesion to host cells, parasite motility, and consequently, its ability to invade host cells. However, the glycoproteome of T. gondii remains largely unknown. In this study, we used the α-mannose-specific Burkholderia cenocepacia lectin A (BC2L-A) to enrich glycopeptides from T. gondii tachyzoites and analysed them by tandem mass spectrometry. The data enable the identification of over 100 N-glycoproteins with the glycosylation site(s) and the composition of the N-glycans at each site. T. gondii glycoproteins include known virulence factors, vaccine candidate
SUBMITTER: Horn V
PROVIDER: S-EPMC12019905 | biostudies-literature | 2025 Apr
REPOSITORIES: biostudies-literature
ACCESS DATA