Abstract

The major aim of this study was to characterize a soluble Plasmodium falciparum antigen from the plasma of malaria-infected humans and Plasmodium falciparum culture supernatants, using immunoabsorbent techniques and Western blotting. An Mr 60-kDa protein was isolated from the plasma of patients with Plasmodium falciparum malaria by affinity chromatography using rabbit anti-Proteus spp GDH(NADP+) serum as ligand. This protein, present in plasma of patients with acute Plasmodium falciparum infection, in Plasmodium falciparum culture supernatants, and in immune complexes, was tested with Plasmodium falciparum malaria hyperimmune serum from patients living in hyperendemic areas and rabbit anti-Proteus spp GDH(NADP+) serum prepared in the laboratory. In this report, we describe the results of a study showing that parasite GDH(NADP+) can be used to detect the presence of Plasmodium falciparum. It appears that this technique permits the chromatographic detection of a Plasmodium falciparum excretion antigen that may be used in the production of monoclonal antibodies to improve immunodiagnostic assays for the detection of antigenemia, and opens the possibility of its use as a non-microscopic screening method.

Highlights

  • Malaria is still one of the most important and devastating tropical diseases, and Plasmodium falciparum kills about 2-3 million people per year [1]

  • The result (Figure 2a) shows that the parasite excretes a protein which is recognized by anti-Proteus spp GDH (NADP+) serum/anti-rabbit IgG peroxidase, that corresponded to a protein with Mr of approximately 60 kDa

  • The main purpose of the present study was to identify the products of excretion that could be associated with infection by Plasmodium falciparum

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Summary

Introduction

Malaria is still one of the most important and devastating tropical diseases, and Plasmodium falciparum kills about 2-3 million people per year [1]. It may be stated that the parasite has a metabolism similar to the host, but the characteristics of many enzymes compromised in these pathways have been considered to be different. Among these enzymes, this study will concentrate on glutamate dehydrogenase whose presence was suspected on the basis of appearance of an Mr 60-kDa band whose enzymatic activity was confirmed by means of an enzymatic assay (RodríguezAcosta A, Gamboa de DN, Aguilar I and Girón ME, unpublished data). In that study we detected the enzymatic activity of Plas-

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