Terminal galactosylation of glycoconjugates in Plasmodium falciparum asexual blood stages and Trypanosoma brucei bloodstream trypomastigotes.

Ramasamy R, Field MC.

Exp Parasitol. 2012 Mar 3

There is definitive biochemical evidence for the presence of terminal α-galactosyl residues (α-gal)

in the N-linked oligosaccharides and glycophosphatidylinositol anchors (GPI anchors) of the variant surface glycoprotein of Trypanosoma brucei bloodstream trypomastigotes. Indirect evidence also exists for α-gal in Plasmodium falciparum asexual blood stage glycoproteins and glycolipids. The occurrence of α-gal in glycoproteins and glycolipids of T. brucei bloodstream trypomastigotes and P. falciparum late asexual blood stages was investigated by the binding of α-gal-specific Bandeirea simplicifolia B4 lectin 1 (BSB4), incorporation of [(3)H] galactose from UDP-[(3)H]galactose into glycoproteins and glycolipids in microsomes in vitro, and bioinformatic searches for galactosyl transferase coding sequences. The findings confirm the presence of α-gal in a spectrum of T. brucei bloodstream trypomastigote glycoproteins and glycolipids and indicate its relative absence from P. falciparum asexual blood stage glycoconjugates.

Correspondence: Professor Ranjan Ramasamy, Institute of Health Sciences, Universiti Brunei Darussalam, Gadong, Brunei Darussalam.