Proteomics

Dataset Information

0

TgPOFUT2 mediated glycosylation


ABSTRACT: Characterisation of glycosylation events within the key adhesin MIC2 of Toxoplasma gondii and the confirmation of tgPOFUT2 as being responsible for Fucosylation of MIC2

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive

ORGANISM(S): Toxoplasma Gondii Gt1

SUBMITTER: Nichollas Scott  

LAB HEAD: Nichollas Scott

PROVIDER: PXD010714 | Pride | 2018-12-04

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
LFQ_proteome_analysis.zip Other
MIC2_GluC.zip Other
MIC2_double_digest.zip Other
MIC2_ingel_trypsin.zip Other
MIC2_trypsin.zip Other
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Publications

Protein <i>O</i>-fucosyltransferase 2-mediated <i>O</i>-glycosylation of the adhesin MIC2 is dispensable for <i>Toxoplasma gondii</i> tachyzoite infection.

Khurana Sachin S   Coffey Michael J MJ   John Alan A   Uboldi Alessandro D AD   Huynh My-Hang MH   Stewart Rebecca J RJ   Carruthers Vern B VB   Tonkin Christopher J CJ   Goddard-Borger Ethan D ED   Scott Nichollas E NE  

The Journal of biological chemistry 20181204 5


<i>Toxoplasma gondii</i> is a ubiquitous, obligate intracellular eukaryotic parasite that causes congenital birth defects, disease in immunocompromised individuals, and blindness. Protein glycosylation plays an important role in the infectivity and evasion of immune responses of many eukaryotic parasites and is also of great relevance to vaccine design. Here we demonstrate that micronemal protein 2 (MIC2), a motility-associated adhesin of <i>T. gondii</i>, has highly glycosylated thrombospondin  ...[more]

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