Abstract
The soluble amphiphilic glycoprotein, Ag1 (gp60), purified from supernatants of in vitro cultures ofPlasmodium falciparum has a molecular mass of 60 kDa and did not exhibit size variation in the differentP. falciparum isolates tested by immunoblotting. Ag1 was shown to interact with the lectinErythrina christagalli agglutinin, which is specific for carbohydrates bearing β-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 antigenspecific manner.
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Jakobsen, P.H., Jepsen, S., Riley, E.M. et al. Biochemical characterization, localization and immunostimulating properties of a soluble glycoprotein, Ag1, isolated from in vitro cultures ofPlasmodium falciparum . Parasitol Res 76, 657–661 (1990). https://doi.org/10.1007/BF00931083
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DOI: https://doi.org/10.1007/BF00931083