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Identification of the fragment containing cross-reacting antigenic determinants in the variable surface glycoprotein of Trypanosoma brucei

Published online by Cambridge University Press:  06 April 2009

A. F. Barbet ,
A. J. Musoke ,
S. Z. Shapiro ,
G. Mpimbaza  and
T. C. McGuire
A. F. Barbet
Affiliation:
International Laboratory for Research on Animal Diseases [ILRAD], P.O. Box 30709, Nairobi Kenya
A. J. Musoke
Affiliation:
International Laboratory for Research on Animal Diseases [ILRAD], P.O. Box 30709, Nairobi Kenya
S. Z. Shapiro
Affiliation:
International Laboratory for Research on Animal Diseases [ILRAD], P.O. Box 30709, Nairobi Kenya
G. Mpimbaza
Affiliation:
International Laboratory for Research on Animal Diseases [ILRAD], P.O. Box 30709, Nairobi Kenya
T. C. McGuire
Affiliation:
Department of Microbiology and Pathology College of Veterinary Medicine, Washington State University, Pullman Washington 99164
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Summary

125I-labelled, isolated variable surface glycoproteins (VSGs) of Trypanosoma b. brucei bind both homologous and heterologous anti-VSG sera and binding to heterologous antisera may be blocked by other unlabelled VSGs (Barbet & McGuire, 1978). This paper presents results which suggest that oligosaccharide residues have importance in the antigenic structure of VSG cross-reacting determinants. The ability of VSG to bind heterologous anti-VSG sera was destroyed by periodate oxidation but not by extensive proteolysis. A VSG glycopeptide fragment was isolated from two different VSGs, which blocked by 100 % the binding of VSG to heterologous anti-VSG sera and therefore contained the cross-reacting determinants. The native glycopeptide fragment was resistant to digestion with trypsin, pronase or leucine aminopeptidase and prolidase. We also show that a VSG synthesized in the reticulocyte lysate cell-free system was not immunoprecipitated by heterologous anti-VSG sera in contrast to the same VSG labelled by metabolic incorporation of [35S]methionine in vivo.

Type
Research Article
Information
Parasitology , Volume 83 , Issue 3 , December 1981 , pp. 623 - 637
Copyright
Copyright © Cambridge University Press 1981

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