Protein O-fucosyltransferase 2–mediated O-glycosylation of the adhesin MIC2 is dispensable for Toxoplasma gondii tachyzoite infection

• Published in: The Journal of biological chemistry Vol. 294; no. 5; pp. 1541 - 1553
• Main Authors: Khurana, Sachin, Coffey, Michael J., John, Alan, Uboldi, Alessandro D., Huynh, My-Hang, Stewart, Rebecca J., Carruthers, Vern B., Tonkin, Christopher J., Goddard-Borger, Ethan D., Scott, Nichollas E.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.02.2019; American Society for Biochemistry and Molecular Biology
• Subjects: Cells, Cultured; Fibroblasts - cytology; Fibroblasts - metabolism; Fibroblasts - parasitology; fucosyltransferase; Fucosyltransferases - metabolism; Glycobiology and Extracellular Matrices; Glycosylation; Host-Parasite Interactions; Humans; Membrane Proteins - metabolism; Proteome - analysis; proteomics; Protozoan Proteins - metabolism; Toxoplasma - pathogenicity; Toxoplasma gondii; Toxoplasmosis - metabolism; Toxoplasmosis - parasitology; glycosylation; fucosyltransferase; Toxoplasma gondii; proteomics; MS

Toxoplasma gondii 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 a...