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Identification, purification and properties of clone-specific glycoprotein antigens constituting the surface coat of Trypanosoma brucei

Published online by Cambridge University Press:  06 April 2009

G. A. M. Cross
G. A. M. Cross
Affiliation:
Medical Research Council Biochemical Parasitology Unit, Molteno Institute, Downing Street, Cambridge CB2 3EE
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Extract

Soluble glycoproteins have been purified from a series of clones of Trypanosoma brucei 427. Each clone yielded a characteristic predominant glycoprotein which induced clone-specific immunity to trypanosome infection in mice. These glycoproteins were shown by specific labelling and enzyme digestion of cells to be the major components of the trypanosome surface coat. Each glycoprotein consisted of a single polypeptide chain having an apparent molecular weight of 65000 (as measured by SDS-polyacrylamide gel electrophoresis) and containing around 600 amino acid and 20 monosaccharide residues. Preliminary structural studies indicated large changes in amino acid sequence dispersed over a considerable length of the polypeptide chain. Proteolytic activity was demonstrated in semi-purified trypanosome extracts, providing one reason for the heterogeneity sometimes observed in surface glycoprotein antigen preparations.

Type
Research Article
Information
Parasitology , Volume 71 , Issue 3 , December 1975 , pp. 393 - 417
Copyright
Copyright © Cambridge University Press 1975

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