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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