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

Afdeling for Klinisk Immunologi DIA

5 Citationer (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.

Originalsprog	Engelsk
Tidsskrift	Parasitology Research
Vol/bind	76
Udgave nummer	8
Sider (fra-til)	657-61
Antal sider	5
ISSN	0932-0113
Status	Udgivet - 1990

Citationsformater

@article{1829b7bdf1ca48e482fa2f4f0dc4238e,

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.",

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",

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",

year = "1990",

language = "English",

volume = "76",

pages = "657--61",

journal = "Parasitology Research",

issn = "0932-0113",

publisher = "Springer Science and Business Media Deutschland GmbH",

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

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.

KW - Animals

KW - Antigens, Protozoan

KW - Antigens, Surface

KW - Fluorescent Antibody Technique

KW - Glycoproteins

KW - Immune Sera

KW - Immunoblotting

KW - Immunoelectrophoresis, Two-Dimensional

KW - Lymphocyte Activation

KW - Malaria

KW - Plasmodium falciparum

KW - Precipitin Tests

KW - Protozoan Proteins

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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