Characterization of a small variable surface glycoprotein from Trypanosoma vivax
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Molecular and Biochemical Parasitology;82(1): 1-11
Permanent link to this item: http://hdl.handle.net/10568/29266
Several biochemical properties of a variant surface glycoprotein (VSG) from the parasite Trypanosoma (Duttonella) vivax have been determined. ILDat 2.1 VSG is approximately 40 kDa in size making this the smallest trypanosome VSG described to date. The glycolipid anchor of ILDat 2.1 VSG is resistant to treatment with T. brucei-derived phospholipase C and data based on lectin affinity chromatography, incorporation of radiolabelled sugar and treatment with endoglycosidase H suggest that the T. vivax VSG bears little carbohydrate. cDNA to ILDat 2.1 VSG mRNA has been cloned and the encoded protein sequence includes the N-terminal amino acid peptide sequence derived from native VSG. The molecular weight of the VSG predicted from the translated cDNA sequence is similar to that of the native molecule and in support of the biochemical data it is devoid of sites for N-linked glycosylation. Examination of the deduced ILDat 2.1 VSG protein sequence reveals that it is most similar to T. congolense VSGs in the distribution of Cys residues and like the former it does not contain any of the defined VSG C-terminal domain types. However, unlike T. congolense VSGs it does not readily fit into the currently described VSG N-terminal domain types. Our studies suggest that IlDat 2.1 VSG is distinct from any of the previously characterized VSGs.