Volume 44, Issue 3
  • ISSN: 0002-9637
  • E-ISSN: 1476-1645



A method for purification of a recombinant protein produced in and its use in an enzyme-linked immunosorbent assay (ELISA) is described. The cloned gene fragment encodes GLURP, the carboxy-terminal 783 amino acid residue portion of a 1271 amino acid residue tamate ich rotein (GLURP), with a molecular weight of 220 kilodalton. The protein is associated with all parasite stages in the human host.

Examination of sera from 105 adult Liberians living in a malaria endemic area revealed anti-GLURP IgG antibodies in 98% of the sera.

The recombinant GLURP was expressed as a chimeric protein, fused with β-galactosidase. However, antibodies in sera were directed only against the malaria part of the fusion protein and not against β-galactosidase.

Antigen from in vitro cultures of isolates from Tanzania (F32), Papua New Guinea (MAD20) and Honduras (HB3) completely absorbed specific antibodies, indicating the presence of conserved epitopes produced by all isolates of .

Recombinant GLURP ELISA is sensitive and rapid, and therefore well-suited for sero-epidemiological studies, and for control of the immunogenicity of a possible future vaccine utilizing epitopes from GLURP.


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