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

P H Jakobsen; S Jepsen; E M Riley; T G Theander; P Grellier; A Lihme; L Hviid; M Dziegiel; J Schrevel

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

P H Jakobsen, S Jepsen, E M Riley, T G Theander, P Grellier, A Lihme, L Hviid, M Dziegiel, J Schrevel

Department of Immunology and Microbiology

5 Citations (Scopus)

Abstract

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 language	English
Journal	Parasitology Reseach
Volume	76
Issue number	8
Pages (from-to)	657-61
Number of pages	4
ISSN	0932-0113
Publication status	Published - 1990

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

abstract = "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.",

author = "Jakobsen, {P H} and S Jepsen and Riley, {E M} and Theander, {T G} and P Grellier and A Lihme and L Hviid and M Dziegiel and J Schrevel",

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",

year = "1990",

language = "English",

volume = "76",

pages = "657--61",

journal = "Parasitology Research",

issn = "0932-0113",

publisher = "Springer",

number = "8",

}

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

SN - 0932-0113

VL - 76

SP - 657

EP - 661

JO - Parasitology Research

JF - Parasitology Research

IS - 8

ER -

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

Abstract

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