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DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2018-09-11
  • AnnouncementXML: Submission_2018-09-11_00:34:12.xml
  • DigitalObjectIdentifier:
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Unsupported dataset by repository
  • PrimarySubmitter: Giulia Bandini
  • Title: Toxoplasma gondii MIC2 TSRs glycosylation
  • Description: Toxoplasma gondii is an intracellular parasite that causes disseminated infections which can lead to neurological damage in fetuses and immunocompromised individuals. Microneme protein 2 (MIC2), a member of the thrombospondin-related anonymous protein (TRAP) family, is a secreted protein important for motility, host cell attachment, invasion, and egress. MIC2 contains six thrombospondin type I repeats (TSRs) that are modified by C-mannose and O-fucose in Plasmodium spp. and mammals. Here we used mass spectrometry to show that the four TSRs in T. gondii MIC2 with protein O-fucosyltransferase 2 (POFUT2) acceptor sites are modified by a dHexHex disaccharide, while Trp residues within three TSRs are also modified with C-mannose. Disruption of genes encoding either pofut2 or nucleotide sugar transporter 2 (nst2), the putative GDP-fucose transporter, results in loss of MIC2 O-fucosylation, as detected by an antibody against the GlcFuc disaccharide, and markedly reduced cellular levels of MIC2. Furthermore, in 10-15% of the Δpofut2 or Δnst2 vacuoles, MIC2 accumulates earlier in the secretory pathway rather than localizing to micronemes. Dissemination of tachyzoites in human foreskin fibroblasts is reduced in these knockouts, which both show defects in attachment to and invasion of host cells comparable to the phenotype observed in the Δmic2. These results, which show O-fucosylation of TSRs is required for efficient processing of MIC2 and for normal parasite invasion, are consistent with the recent demonstration that P. falciparum Δpofut2 has decreased virulence and support a conserved role for this glycosylation pathway in quality control of TSR-containing proteins in eukaryotes.
  • SpeciesList: scientific name: Toxoplasma gondii RH; NCBI TaxID: 383379; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
  • ModificationList: monohydroxylated residue; deoxyhexosylated; iodoacetamide derivatized residue; hexosylated residue
  • Instrument: Q Exactive; LTQ Orbitrap

Dataset History

VersionDatetimeStatusChangeLog Entry
02018-07-31 01:46:36ID requested
12018-08-09 09:49:53announced
22018-09-11 00:34:12announcedUpdated project metadata.

Publication List

  1. Dataset with its publication pending

Keyword List

  1. curator keyword: Biomedical
  2. submitter keyword: O-fucosylation, C-mannosylation, Toxoplasma gondii

Contact List

    Catherine Elizabeth Costello
    • contact affiliation: Department of Biochemistry, Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, MA 02118, USA
    • contact email: cecmsms@bu.edu
    • lab head:
    Giulia Bandini
    • contact affiliation: Boston University
    • contact email: gbandini@bu.edu
    • dataset submitter:

Full Dataset Link List

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  2. PRIDE project URI
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