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      Plasmodium chabaudi: immunogenicity of a highly antigenic glutamate-rich protein.

      Experimental Parasitology
      Animals, Antibodies, Protozoan, analysis, immunology, Antigens, Protozoan, chemistry, DNA, Protozoan, Erythrocytes, parasitology, Fluorescent Antibody Technique, Glutamic Acid, Immunoblotting, Malaria, prevention & control, Mice, Molecular Weight, Parasitemia, Plasmodium chabaudi, Protozoan Proteins, Protozoan Vaccines, Recombinant Proteins, Repetitive Sequences, Nucleic Acid, Sequence Homology, Amino Acid, Vaccines, Synthetic

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          Abstract

          The immunogenicity of a 93-kDa Plasmodium chabaudi protein that contains glutamate-rich tandem repeats was investigated in this study. Immunoblotting with various monoclonal antibodies indicates that this 93-kDa protein is equivalent to a potential P. chabaudi RESA analogue. However, the sequence of the P. chabaudi protein does not exhibit any significant homology to Pf155/RESA. Antibodies against the 93-kDa protein appear early during P. chabaudi infection and reach high titers. The highest antibody titers are found when the parasitemia is descending, suggesting that this protein may play some role in immunity. Immunization of mice with the recombinant protein also results in high antibody titers, indicating that the protein is quite immunogenic. However, mice immunized with recombinant protein and challenged with P. chabaudi do not exhibit a delayed appearance of parasitemia, a reduced parasitemia, or a shortened duration of parasitemia. Glutamate-rich P. falciparum proteins such as Pf155/RESA, are being considered as vaccine candidates. The studies with P. chabaudi suggest that interpretation of serological data using glutamate-rich proteins should proceed with caution. The glutamate-rich repeats, although highly immunogenic, may not be important in host immunity against malaria. However, antibodies that appear late in the P. chabaudi infection do appear to play a role in anti-malarial immunity.

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