Biochemistry. 2008 Nov 1. [Epub ahead of print]
The Dual Origin of Toxoplasma gondii N-Glycans
Garénaux E, Shams-Eldin H, Chirat F, Bieker U, Schmidt J, Michalski JC, Cacan R, Guérardel Y, Schwarz RT.
Unite de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, Universite des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France, and Institut fur Virologie, AG Parasitologie, Philipps-Universitat Marburg, Hans-Meerwein-Strasse 2, 35043 Marburg, Germany email@example.com.
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.
PMID: 18975916 [PubMed - as supplied by publisher]