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Clinical and Diagnostic Laboratory Immunology, Jan 1995, 30-34, Vol 2, No. 1
M Theisen, J Vuust, A Gottschau, S Jepsen and B Hogh
A recombinant Plasmodium falciparum glutamate-rich protein (GLURP) was
produced in Escherichia coli as a nearly full-length protein. In order to
map immunodominant regions on GLURP, the nonrepetitive amino- terminal
region (R0) as well as the central repeat region (R1) and the
carboxy-terminal repeat region (R2) were also produced as separate
products. All four purified gene products reacted specifically with serum
samples from adults living in an area of Liberia where malaria is
holoendemic. It appears that the human immune response against GLURP is
primarily directed against the R2 region because 94% of the serum samples
reacted with this region in an immunoassay. Antibody reactivity against the
R0 region was also observed in 75% of the serum samples, while the R1
region showed only weak antibody-binding activity. When the nearly
full-length GLURP molecule was adsorbed to Al(OH)3 it was found to be
immunogenic in mice. In these experiments, the antibody response was almost
exclusively directed against the R2 region. When anti-GLURP sera were
obtained from rabbits immunized with the three regions, R0, R1, and R2,
respectively, they recognized in immunoprecipitation experiments authentic
GLURP from P. falciparum grown in vitro. These results demonstrate that
GLURP produced in E. coli can induce a humoral immune response against
GLURP derived from blood-stage parasites.
Copyright © 1995 by the American Society for Microbiology. All rights reserved.
Antigenicity and immunogenicity of recombinant glutamate-rich protein of Plasmodium falciparum expressed in Escherichia coli
Department of Infection-Immunology, Statens Seruminstitut, Copenhagen S, Denmark.
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