Biochemical characterization, localization and immunostimulating properties of a soluble glycoprotein, Ag1, isolated from in vitro cultures of Plasmodium falciparum

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The soluble amphiphilic glycoprotein, Ag1 (gp60), purified from supernatants of in vitro cultures of Plasmodium falciparum has a molecular mass of 60 kDa and did not exhibit size variation in the different P. falciparum isolates tested by immunoblotting. Ag1 was shown to interact with the lectin Erythrina christagalli agglutinin, which is specific for carbohydrates bearing beta-D-galactose(1-4)-D-N-acetylglucosamine. Indirect immunofluorescence studies showed that Ag1 is located on the surface of trophozoites and schizonts but not on the surface of merozoites. Ag1 is recognized by human immune sera from six different malaria-endemic regions. Ag1 induces in vitro proliferation of lymphocytes from malaria-immune individuals in an antigen-specific manner.
Original languageEnglish
JournalParasitology Reseach
Issue number8
Pages (from-to)657-61
Number of pages4
Publication statusPublished - 1990

Bibliographical note

Keywords: Animals; Antigens, Protozoan; Antigens, Surface; Fluorescent Antibody Technique; Glycoproteins; Immune Sera; Immunoblotting; Immunoelectrophoresis, Two-Dimensional; Lymphocyte Activation; Malaria; Plasmodium falciparum; Precipitin Tests; Protozoan Proteins

ID: 6748632