Characterization of Naturally Acquired Human IgG Responses against the N-Terminal Region of the Merozoite Surface Protein 1 of Plasmodium vivax

Gabriela LevitusDepartmento de Parasitologia, Universidade de Sao Paulo, Sao Paulo, Brazil

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Frederic MertensDepartmento de Parasitologia, Universidade de Sao Paulo, Sao Paulo, Brazil

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Marcia A. SperancaDepartmento de Parasitologia, Universidade de Sao Paulo, Sao Paulo, Brazil

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Luis Marcelo Aranha CamargoDepartmento de Parasitologia, Universidade de Sao Paulo, Sao Paulo, Brazil

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Marcelo Urbano FerreiraDepartmento de Parasitologia, Universidade de Sao Paulo, Sao Paulo, Brazil

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Hernando A. Del PortilloDepartmento de Parasitologia, Universidade de Sao Paulo, Sao Paulo, Brazil

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The primary structure of the merozoite surface protein 1 of Plasmodium vivax (PvMSP-1) revealed the existence of conserved and polymorphic blocks of the protein among different Plasmodium species. To characterize the naturally acquired IgG antibody responses to the PvMSP-1 molecule, the entire N-terminal portion of this protein was expressed as 10 overlapping glutathione S-transferase fusion proteins. The affinity-purified recombinant products were tested by enzyme-linked immunosorbent assay and Western blot against the sera of malaria patients from the state of Rondonia, Brazil. We found that the majority of these sera did not contain IgG antibodies recognizing recombinant proteins expressing exclusively interspecies conserved blocks of the molecule. In contrast, a high proportion of these same sera reacted against recombinant products expressing interspecies polymorphic regions of this protein. The poor B cell immunogenicity of the interspecies conserved blocks of the PvMSP-1 molecule most likely reflects important and unknown structural or functional features of these regions.

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