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  • Title: Structural analysis of the asparagine-linked glycans from the procyclic Trypanosoma brucei and its glycosylation mutants resistant to Concanavalin A killing.
    Author: Hwa KY, Khoo KH.
    Journal: Mol Biochem Parasitol; 2000 Nov; 111(1):173-84. PubMed ID: 11087927.
    Abstract:
    The variant surface glycoprotein of the bloodstream form of Trypanosoma brucei is known to be glycosylated with a range of structures including high mannose and complex types. In contrast, glycosylation in the procyclic form of the parasite appears to be restricted to a single Man(5)GlcNAc(2) structure, as found on its procyclin. To gain a better insight into the developmentally regulated glycosylation pattern, we have structurally defined the full range of N-linked glycans made by the procyclic trypanosomes, as well as two previously described glycosylation mutants generated under Con A selection. It was found that the wild type procyclic cells could synthesize a full range of high mannose type structures from Man(5)GlcNAc(2) to Man(9)GlcNAc(2), with Man(5)GlcNAc(2) as the major component. In contrast, the two mutants mainly synthesized a truncated Man(4)GlcNAc(2) structure, Man alpha 1-3Man alpha 1-6(Man alpha1-3)Man be ta 1-4 GlcNAc beta 1-4GlcNAc, a significant portion of which was further extended by a single GlcNAc to form GlcNAc-Man(4)GlcNAc(2) and a single N-acetyllactosamine unit at the 3-arm position to form Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3(Man al pha 1- 3Man alpha 1-6)Man beta 1-4G lcNAc beta 1-4GlcNAc. The results suggest that the procyclic trypanosomes could be induced by Con A selection to synthesize limited hybrid type structures, but in general do not further process their N-linked glycans into multiantennary complex types as the blood stream forms do.
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