Capture ELISA for IgM antibodies against Plasmodium falciparum glutamate rich protein

Morten Hanefeld Dziegiel; M B Borre; E Petersen; B Högh; S Jepsen; J Vuust; N Axelsen

Capture ELISA for IgM antibodies against Plasmodium falciparum glutamate rich protein

Morten Hanefeld Dziegiel, M B Borre, E Petersen, B Högh, S Jepsen, J Vuust, N Axelsen

3 Citationer (Scopus)

Abstract

This report describes a novel mu chain capture ELISA for the detection of IgM antibodies against a Plasmodium falciparum antigen. A fragment of the 220 kDa P. falciparum glutamate rich protein containing amino acid residues 489-1271 was expressed in E. coli as a recombinant chimeric beta-galactosidase fusion protein and used as antigen after purification and biotinylation. Specific IgM antibodies were found in 51% (39/77) of sera from adult Liberians immune to malaria. The binding of IgM antibodies was specific for the malaria portion of the fusion protein and no cross-reactivity was found in sera from patients with IgM antibodies due to other diseases. Inhibition studies with a fusion protein containing amino acid residues 816-1134 (GLURP816-1134) representing the carboxy-terminal repeat region suggested a different use of epitopes for IgM antibodies in different individuals.

Originalsprog	Engelsk
Tidsskrift	Journal of Immunological Methods
Vol/bind	155
Udgave nummer	2
Sider (fra-til)	207-13
Antal sider	7
ISSN	0022-1759
Status	Udgivet - 5 nov. 1992

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Citationsformater

@article{8029b41d62b147aba86c536200883d90,

title = "Capture ELISA for IgM antibodies against Plasmodium falciparum glutamate rich protein",

abstract = "This report describes a novel mu chain capture ELISA for the detection of IgM antibodies against a Plasmodium falciparum antigen. A fragment of the 220 kDa P. falciparum glutamate rich protein containing amino acid residues 489-1271 was expressed in E. coli as a recombinant chimeric beta-galactosidase fusion protein and used as antigen after purification and biotinylation. Specific IgM antibodies were found in 51% (39/77) of sera from adult Liberians immune to malaria. The binding of IgM antibodies was specific for the malaria portion of the fusion protein and no cross-reactivity was found in sera from patients with IgM antibodies due to other diseases. Inhibition studies with a fusion protein containing amino acid residues 816-1134 (GLURP816-1134) representing the carboxy-terminal repeat region suggested a different use of epitopes for IgM antibodies in different individuals.",

keywords = "Animals, Antibodies, Protozoan, Antigens, Protozoan, Enzyme-Linked Immunosorbent Assay, Humans, Immunoglobulin M, Malaria, Falciparum, Plasmodium falciparum, Protozoan Proteins",

author = "Dziegiel, {Morten Hanefeld} and Borre, {M B} and E Petersen and B H{\"o}gh and S Jepsen and J Vuust and N Axelsen",

year = "1992",

month = nov,

day = "5",

language = "English",

volume = "155",

pages = "207--13",

journal = "Journal of Immunological Methods",

issn = "0022-1759",

publisher = "Elsevier",

number = "2",

}

TY - JOUR

T1 - Capture ELISA for IgM antibodies against Plasmodium falciparum glutamate rich protein

AU - Dziegiel, Morten Hanefeld

AU - Borre, M B

AU - Petersen, E

AU - Högh, B

AU - Jepsen, S

AU - Vuust, J

AU - Axelsen, N

PY - 1992/11/5

Y1 - 1992/11/5

N2 - This report describes a novel mu chain capture ELISA for the detection of IgM antibodies against a Plasmodium falciparum antigen. A fragment of the 220 kDa P. falciparum glutamate rich protein containing amino acid residues 489-1271 was expressed in E. coli as a recombinant chimeric beta-galactosidase fusion protein and used as antigen after purification and biotinylation. Specific IgM antibodies were found in 51% (39/77) of sera from adult Liberians immune to malaria. The binding of IgM antibodies was specific for the malaria portion of the fusion protein and no cross-reactivity was found in sera from patients with IgM antibodies due to other diseases. Inhibition studies with a fusion protein containing amino acid residues 816-1134 (GLURP816-1134) representing the carboxy-terminal repeat region suggested a different use of epitopes for IgM antibodies in different individuals.

AB - This report describes a novel mu chain capture ELISA for the detection of IgM antibodies against a Plasmodium falciparum antigen. A fragment of the 220 kDa P. falciparum glutamate rich protein containing amino acid residues 489-1271 was expressed in E. coli as a recombinant chimeric beta-galactosidase fusion protein and used as antigen after purification and biotinylation. Specific IgM antibodies were found in 51% (39/77) of sera from adult Liberians immune to malaria. The binding of IgM antibodies was specific for the malaria portion of the fusion protein and no cross-reactivity was found in sera from patients with IgM antibodies due to other diseases. Inhibition studies with a fusion protein containing amino acid residues 816-1134 (GLURP816-1134) representing the carboxy-terminal repeat region suggested a different use of epitopes for IgM antibodies in different individuals.

KW - Animals

KW - Antibodies, Protozoan

KW - Antigens, Protozoan

KW - Enzyme-Linked Immunosorbent Assay

KW - Humans

KW - Immunoglobulin M

KW - Malaria, Falciparum

KW - Plasmodium falciparum

KW - Protozoan Proteins

M3 - Journal article

C2 - 1431149

SN - 0022-1759

VL - 155

SP - 207

EP - 213

JO - Journal of Immunological Methods

JF - Journal of Immunological Methods

IS - 2

ER -

Capture ELISA for IgM antibodies against Plasmodium falciparum glutamate rich protein

Abstract

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