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Trypanosoma cruzi cells undergo an alteration in protein N-glycosylation upon differentiation

Journal Article · · J. Biol. Chem.; (United States)
OSTI ID:6086066
Trypanosoma cruzi epimastigotes (insect gut stage) incubated with (U- UC)glucose synthesized Man9GlcNAc2-P-P-dolichol as practically the sole dolichol-P-P derivative. On the other hand, amastigotes (intracellular stage) of the same parasite synthesized four to five times more Man7GlcNAc2-P-P-dolichol than Man9GlcNAc2-P-P-dolichol. Evidence is presented indicating that, whereas in epimastigotes only Man9GlcNAc2 was transferred to proteins, in amastigotes both Man7GlcNAc2 and Man9GlcNAc2 were transferred in direct proportion to their respective amounts bound to dolichol-P-P. The change in the mechanism of protein N-glycosylation could be observed upon in vitro differentiation of amastigotes to epimastigotes. The dissimilar size of the main oligosaccharides transferred to proteins in epimastigotes and amastigotes was responsible for differences in two structural features of high mannose-type oligosaccharides present in mature glycoproteins of both forms of the parasite, namely the average size of the compounds and the structure of the main species of some isomer oligosaccharides.
Research Organization:
Instituto Nacional del Diagnostico e Investigacion de la Enfermedad de Chagas, Buenos Aires, Argentina
OSTI ID:
6086066
Journal Information:
J. Biol. Chem.; (United States), Journal Name: J. Biol. Chem.; (United States) Vol. 18; ISSN JBCHA
Country of Publication:
United States
Language:
English

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