Abstract
We have previously shown that only a single 19-kDa fragment of the Plasmodium falciparum major merozoite surface protein (MSP1) is carried with an invading merozoite into the infected red cell. This fragment (MSP1(19] is derived from the C-terminal membrane-bound end of a major product, MSP1(42), of the primary stage of MSP1 proteolytic processing. Using a monoclonal antibody mapped to an epitope within the N-terminal region of MSP1(42), we have shown that a soluble 33-kDa polypeptide (MSP1(33) corresponding to the N-terminal region of MSP1(42) is shed into culture supernatants during merozoite release and erythrocyte invasion. These observations provide further evidence that the secondary processing of MSP1(42) involves a highly site-specific proteolytic activity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antibodies, Monoclonal
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Antigens, Protozoan / genetics
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Antigens, Surface / genetics
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Epitopes / genetics
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Erythrocytes / parasitology
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Merozoite Surface Protein 1
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Molecular Weight
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Peptide Fragments / genetics
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Peptide Fragments / immunology
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Peptide Fragments / metabolism
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Plasmodium falciparum / genetics
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Plasmodium falciparum / immunology
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Plasmodium falciparum / metabolism*
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Protein Precursors / genetics
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Protein Precursors / immunology
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Protein Precursors / metabolism*
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Protein Processing, Post-Translational
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Protozoan Proteins / genetics
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Protozoan Proteins / immunology
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Protozoan Proteins / metabolism*
Substances
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Antibodies, Monoclonal
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Antigens, Protozoan
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Antigens, Surface
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Epitopes
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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