Identification of a strain-specific malarial antigen exposed on the surface of Plasmodium falciparum-infected erythrocytes
Autor: | J H Leech, Louis H. Miller, Russell J. Howard, John W. Barnwell |
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Jazyk: | angličtina |
Rok vydání: | 1984 |
Předmět: |
Erythrocytes
Immunology Plasmodium falciparum KAHRP Biology chemistry.chemical_compound Antigen Species Specificity medicine Cell Adhesion Immunology and Allergy Animals Trypsin Sodium dodecyl sulfate Melanoma Immunosorbent Techniques chemistry.chemical_classification Immune Sera Membrane Proteins Articles biology.organism_classification Molecular biology Amino acid Molecular Weight Red blood cell medicine.anatomical_structure Membrane protein chemistry Aotus trivirgatus Antigens Surface medicine.drug |
Zdroj: | The Journal of Experimental Medicine |
ISSN: | 1540-9538 0022-1007 |
Popis: | We have identified strain-specific antigens with Camp and St. Lucia strains of P. falciparum of Mr approximately 285,000 and approximately 260,000, respectively. These strain-specific antigens were metabolically labeled with radioactive amino acids, indicating that they were of parasite origin rather than altered host components. These proteins had the properties of a molecule exposed on the surface of infected erythrocytes (IE). First, the proteins are accessible to lactoperoxidase-catalyzed radioiodination of IE. Second, the radioiodinated proteins were cleaved by low concentrations of trypsin (0.1 microgram/ml). Third, these antigens were immunoprecipitated after addition of immune sera to intact IE. Fourth, the strain-specific immuno-precipitation of these proteins correlated with the capacity of immune sera to block cytoadherence of IE in a strain-specific fashion. Fifth, the strain-specific antigen had detergent solubility properties (i.e., insolubility in 1% Triton X-100, solubility in 5% sodium dodecyl sulfate) similar to the variant antigen of P. knowlesi, which has been proven to be a malarial protein exposed on the erythrocyte surface. |
Databáze: | OpenAIRE |
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