Trypanosoma cruzi cells undergo an alteration in protein N-glycosylation upon differentiation
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), Vol. 18
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
CARBON 14 COMPOUNDS
BIOSYNTHESIS
GLUCOPROTEINS
TRYPANOSOMA
CELL DIFFERENTIATION
GLUCOSE
OLIGOSACCHARIDES
ALDEHYDES
CARBOHYDRATES
HEXOSES
LABELLED COMPOUNDS
MASTIGOPHORA
MONOSACCHARIDES
ORGANIC COMPOUNDS
PARASITES
PROTEINS
SACCHARIDES
SYNTHESIS
550201* - Biochemistry- Tracer Techniques