Abstract
We have expressed in bacteria the C-terminal part of Plasmodium yoelii merozoite surface protein-1 (MSP1) containing the two epidermal growth factor-like domains. The protein, either alone or fused to glutathione S-transferase, was highly effective as a vaccine and protected mice against challenge infection. Reduction and alkylation abolished the protection obtained with the protein. This shows for the first time the absolute requirement of the disulphide-bonded conformation for immunogenicity. In a short term experiment, mice were protected against a massive challenge. The immunity was effective at the time of merozoite release/reinvasion. Recombinant protein based on this part of MSP1 may be suitable as a vaccine against malaria.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Base Sequence
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DNA Primers
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Epidermal Growth Factor / immunology
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Escherichia coli / genetics
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Glutathione Transferase / immunology
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Malaria Vaccines*
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Merozoite Surface Protein 1
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Mice
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Mice, Inbred BALB C
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Molecular Sequence Data
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Peptide Fragments / immunology
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Plasmodium yoelii / immunology*
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Protein Precursors / genetics
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Protein Precursors / immunology
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Protozoan Proteins / genetics
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Protozoan Proteins / immunology
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Recombinant Fusion Proteins / immunology
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Vaccines, Synthetic*
Substances
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DNA Primers
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Malaria Vaccines
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Merozoite Surface Protein 1
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Peptide Fragments
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Protein Precursors
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Protozoan Proteins
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Recombinant Fusion Proteins
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Vaccines, Synthetic
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Epidermal Growth Factor
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Glutathione Transferase