Antigenicity and immunogenicity of recombinant glutamate-rich protein of Plasmodium falciparum expressed in Escherichia coli

• DOI: 10.1128/cdli.2.1.30-34.1995
• Publication Date: 2020-01-06T18:34:32Z
• Authors: M Theisen; J Vuust; A Gottschau; S Jepsen; B Høgh
• Keywords: Antigenicity; Merozoite surface protein

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) well central repeat (R1) and carboxy-terminal (R2) were also separate products. All four purified gene products reacted specifically with serum samples from adults living an area of Liberia where malaria is holoendemic. It appears that human immune response against GLURP primarily directed R2 because 94% this immunoassay. Antibody reactivity R0 observed 75% samples, while R1 showed only weak antibody-binding activity. When molecule adsorbed Al(OH)3 it found be immunogenic mice. these experiments, antibody almost exclusively region. anti-GLURP sera obtained rabbits immunized three regions, R0, R1, R2, respectively, they recognized immunoprecipitation experiments authentic P. grown vitro. These results demonstrate E. can induce humoral derived blood-stage parasites.