POFUT2-mediated O-glycosylation of MIC2 is dispensable for Toxoplasma gondii tachyzoites

Abstract

Toxoplasma gondii is a ubiquitous obligate intracellular eukaryotic parasite that causes congenital birth defects, disease of the immunocompromised and blindness. Protein glycosylation plays an important role in the infectivity and evasion of immune response of many eukaryotic parasites and is also of great relevance to vaccine design. Here, we demonstrate that MIC2, the motility-associated adhesin of T. gondii , has highly glycosylated thrombospondin repeat domains (TSR). At least seven C- linked and three O -linked glycosylation sites exist within MIC2, with >95% occupancy at O -glycosylation sites. We demonstrate that the addition of O -glycans to MIC2 is mediated by a protein O -fucosylt..