Biochemical characterization, localization and immunostimulating properties of a soluble glycoprotein, Ag1, isolated from in vitro cultures of Plasmodium falciparum
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Biochemical characterization, localization and immunostimulating properties of a soluble glycoprotein, Ag1, isolated from in vitro cultures of Plasmodium falciparum. / Jakobsen, P H; Jepsen, S; Riley, E M; Theander, T G; Grellier, P; Lihme, A; Hviid, L; Dziegiel, M; Schrevel, J.
I: Parasitology Reseach, Bind 76, Nr. 8, 1990, s. 657-61.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Biochemical characterization, localization and immunostimulating properties of a soluble glycoprotein, Ag1, isolated from in vitro cultures of Plasmodium falciparum
AU - Jakobsen, P H
AU - Jepsen, S
AU - Riley, E M
AU - Theander, T G
AU - Grellier, P
AU - Lihme, A
AU - Hviid, L
AU - Dziegiel, M
AU - Schrevel, J
N1 - 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
PY - 1990
Y1 - 1990
N2 - 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.
AB - 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.
M3 - Journal article
C2 - 2251241
VL - 76
SP - 657
EP - 661
JO - Parasitology Research
JF - Parasitology Research
SN - 0932-0113
IS - 8
ER -
ID: 6748632