Does a histidine-rich protein from Plasmodium lophurae have a function in merozoite penetration?
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Updated: Aug 3, 2026

High Yield Purification of Plasmodium falciparum Merozoites For Use in Opsonizing Antibody Assays
Published on: July 17, 2014
Abstract:
Autoradiography was used to localize the distribution of L-[3H]histidine incorporated in vitro by developing segmenters of Plasmodium lophurae. Under conditions used for the visualization of high specific activity loci, radioactivity appeared associated mainly with the histidine-rich protein of cytoplasmic granules as well as with rhoptries and micronemes of merozoites. The isolated histidine-rich protein caused agglutination of erythrocytes and increased their osmotic fragility. Based on the observed evidence suggesting the presence of this histidine-rich protein in the polar organelles of merozoites and its reactivity with erythrocyte membranes, the hypothesis that such a protein may have a function in the penetration of merozoites is proposed.
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