The variable surface glycoproteins of Trypanosoma equiperdum are phosphorylated

The phosphoproteins from three Trypanosoma equiperdum variants were studied by labelling the parasites in vivo with 32P. Phosphoprotein analysis reveals the presence of a 58 000 mol. wt. phosphoprotein (pp58) which is absent when live trypanosomes are pre‐treated with proteinase K under conditions w...

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Bibliographic Details
Published in:The EMBO journal 1982-01, Vol.1 (11), p.1393-1398
Main Authors: Baltz, T., Giroud, C., Baltz, D., Duvillier, G., Degand, P., Demaille, J., Pautrizel, R.
Format: Article
Language:English
Subjects:
Animals
Cyanogen Bromide
Glycoproteins - isolation & purification
Immunodiffusion
Molecular Weight
Peptide Fragments - analysis
Phosphopeptides - analysis
Phosphoproteins - isolation & purification
Phosphorylation
Trypanosoma - analysis
Trypanosoma equiperdum
Variant Surface Glycoproteins, Trypanosoma
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Summary:The phosphoproteins from three Trypanosoma equiperdum variants were studied by labelling the parasites in vivo with 32P. Phosphoprotein analysis reveals the presence of a 58 000 mol. wt. phosphoprotein (pp58) which is absent when live trypanosomes are pre‐treated with proteinase K under conditions where only the surface coat containing the variable surface glycoprotein (VSG) is removed. Immunological and fingerprint analysis on labelled pp58, purified from these variants by affinity chromatography on Concanavalin A‐Sepharose, clearly identify this component as the VSG. Furthermore, the VSGs seem to be phosphorylated to the extent of 1 mol phosphate per mol glycoprotein. The phosphorylated region is located in the extreme C‐terminal region representing approximately 10% of the total molecule. The phosphorylated residue is not an aliphatic or aromatic ester of serine, threonine, or tyrosine, nor an acyl phosphate involving an aspartyl or glutamyl residue, nor phosphohistidine. The evidence that VSGs are phosphorylated could have considerable implications for the transfer and function of these structures.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1982.tb01328.x