The dual origin of Toxoplasma gondii N-glycans |
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Authors: | Garénaux Estelle Shams-Eldin Hosam Chirat Frederic Bieker Ulrike Schmidt Jörg Michalski Jean-Claude Cacan René Guérardel Yann Schwarz Ralph T |
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Institution: | Unité de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, Universit des Sciences et Technologies de Lille, 59655 VilleneuVe d'Ascq cedex, France. |
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Abstract: | N-Linked glycosylation is the most frequent modification of secreted proteins in eukaryotic cells that plays a crucial role in protein folding and trafficking. Mature N-glycans are sequentially processed in the endoplasmic reticulum and Golgi apparatus through a pathway highly conserved in most eukaryotic organisms. Here, we demonstrate that the obligate intracellular protozoan parasite Toxoplasma gondii independently transfers endogenous truncated as well as host-derived N-glycans onto its own proteins.Therefore, we propose that the apicomplexan parasite scavenges N-glycosylation intermediates from the host cells to compensate for the rapid evolution of its biosynthetic pathway, which is primarily devoted to modification of proteins with glycosylphosphatidylinositols rather than N-glycans. |
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