Journal of Experimental Medicine, Vol 166, 376-390, Copyright © 1987 by Rockefeller University Press

ARTICLES

Possible pitfalls in the identification of glycophorin-binding proteins of Plasmodium falciparum

MR van Schravendijk, RJ Wilson and CI Newbold

Plasmodium falciparum proteins that bind to the putative erythrocyte receptor (glycophorin) have been identified in several laboratories by their ability to bind to glycophorin immobilized on aminoethyl-BioGel (AE-BioGel). We here report that several parasite proteins bind to AE- BioGel in the absence of coupled glycophorin. Binding is apparently due to the strong ion-exchange properties of the matrix, and is sensitive to ionic conditions such as the degree of equilibration of the matrix and the pH. The parasite proteins that bind to the blank column under appropriate conditions include proteins with the serological activities of S-antigen and Ag 23, which also bind to glycophorin-coupled AE- BioGel. In the light of these results, the glycophorin-binding specificity of these and other proteins reported to bind to glycophorin- coupled AE-BioGel will have to be reevaluated, preferably using a different support matrix.
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This article has been cited by other articles:

• Burghaus, P. A., Lingelbach, K. (2001). Luciferase, When Fused to an N-terminal Signal Peptide, Is Secreted from Transfected Plasmodium falciparum and Transported to the Cytosol of Infected Erythrocytes. J. Biol. Chem. 276: 26838-26845 [Abstract] [Full Text]  

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