The dual origin of Toxoplasma gondii N-glycans.
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.
Garénaux
Estelle
E
Unité de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, Universit des Sciences et Technologies de Lille, 59655 VilleneuVe d'Ascq cedex, France.
Shams-Eldin
Hosam
H
Chirat
Frederic
F
Bieker
Ulrike
U
Schmidt
Jörg
J
Michalski
Jean-Claude
JC
Cacan
René
R
Guérardel
Yann
Y
Schwarz
Ralph T
RT
D000818:Animals; D002460:Cell Line; D006031:Glycosylation; D016695:Glycosyltransferases / Q000172:deficiency / Q000378:metabolism; D006801:Humans; D008358:Mannose / Q000737:chemistry / Q000378:metabolism; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D011134:Polysaccharides / Q000096:biosynthesis* / Q000737:chemistry / Q000378:metabolism*; D015800:Protozoan Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D014122:Toxoplasma / Q000254:growth & development / Q000378:metabolism*
D009844:Oligosaccharides; D011134:Polysaccharides; D015800:Protozoan Proteins; D016695:Glycosyltransferases; D008358:Mannose