+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Interaction of the 140/130/110 kDa rhoptry protein complex of Plasmodium falciparum with the erythrocyte membrane and liposomes



Interaction of the 140/130/110 kDa rhoptry protein complex of Plasmodium falciparum with the erythrocyte membrane and liposomes



Experimental Parasitology 732: 161-171



During Plasmodium falciparum merozoite invasion into human and mouse erythrocytes, a 110-kDa rhoptry protein is secreted from the organelle into the erythrocyte membrane. In the present study our interest was to examine the interaction of rhoptry proteins of P. falciparum with the erythrocyte membrane. It was observed that the complex of rhoptry proteins of 140/130/110 kDa bind directly to a trypsin sensitive site on intact mouse erythrocytes, and not human, saimiri, or other erythrocytes. However, when erythrocytes were disrupted by hypotonic lysis, rhoptry proteins of 140/130/110 kDa were found to bind to membranes and inside-out vesicles prepared from human, mouse, saimiri, rhesus, rat, and rabbit erythrocytes. A binding site on the cytoplasmic face of the erythrocyte membrane suggests that the rhoptry proteins may be translocated across the lipid bilayer during merozoite invasion. Furthermore, pretreatment of human erythrocytes with a specific peptide derived from MSA-1, the major P. falciparum merozoite surface antigen of MW 190,000-200,000, induced binding of the 140/130/110-kDa complex. The rhoptry proteins bound equally to normal human erythrocytes and erythrocytes treated with neuraminidase, trypsin, and chymotrypsin indicating the binding site was independent of glycophorin and other major surface proteins. The rhoptry protein complex also bound specifically to liposomes prepared from different types of phospholipids. Liposomes containing PE effectively block binding of the rhoptry proteins to mouse cells, suggesting that there are two binding sites on the mouse membrane for the 140/130/110-kDa complex, one protein and a second, possibly lipid in nature. The results of this study suggest that the 140/130/110 kDa protein complex may interact directly with sites in the lipid bilayer of the erythrocyte membrane.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 002141907

Download citation: RISBibTeXText

PMID: 1889471

DOI: 10.1016/0014-4894(91)90019-s


Related references

Interaction between Plasmodium falciparum apical membrane antigen 1 and the rhoptry neck protein complex defines a key step in the erythrocyte invasion process of malaria parasites. Journal of Biological Chemistry 285(19): 14815-14822, 2010

Plasmodium falciparum: analysis of protein-protein interactions of the 140/130/110-kDa rhoptry protein complex using antibody and mouse erythrocyte binding assays. Experimental Parasitology 77(2): 179-194, 1993

Positive selection on the Plasmodium falciparum clag2 gene encoding a component of the erythrocyte-binding rhoptry protein complex. Tropical Medicine and Health 39(3): 77-82, 2011

Mapping the binding domains involved in the interaction between the Plasmodium falciparum knob-associated histidine-rich protein and the cytoadherence ligand P falciparum erythrocyte membrane protein 1. Journal of Biological Chemistry 274(34): 23808-23813, 1999

Mapping the binding domains involved in the interaction between the Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) and the cytoadherence ligand P. falciparum erythrocyte membrane protein 1 (PfEMP1). Journal of Biological Chemistry 274(34): 23808-23813, 1999

Preferential binding of Plasmodium falciparum SERA and rhoptry proteins to erythrocyte membrane inner leaflet phospholipids. Infection and Immunity 62(4): 1207-1212, 1994

Interaction of Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) with erythrocyte ankyrin R is required for its attachment to the erythrocyte membrane. Biochimica et Biophysica Acta 1838(1 Pt B): 185-192, 2014

A thrombospondin structural repeat containing rhoptry protein from Plasmodium falciparum mediates erythrocyte invasion. Cellular Microbiology 15(8): 1341-1356, 2013

Characterization of a membrane-associated rhoptry protein of Plasmodium falciparum. Journal of Biological Chemistry 279(6): 4648-4656, 2004

The Plasmodium falciparum clag9 gene encodes a rhoptry protein that is transferred to the host erythrocyte upon invasion. Molecular Microbiology 52(1): 107-118, 2004

Specific T-cell recognition of the merozoite proteins rhoptry-associated protein 1 and erythrocyte-binding antigen 1 of Plasmodium falciparum. Infection and Immunity 61(1): 268-273, 1993

Plasmodium falciparum rhoptry protein clag9 is not an erythrocyte surface molecule but has a role in the expression of the cytoadhesion phenotype. Experimental Parasitology 105(1): 57, 2003

Specific erythrocyte binding capacity and biological activity of Plasmodium falciparum-derived rhoptry-associated protein 1 peptides. Vaccine 22(8): 1054-1062, 2004

A peptide derived from a B cell epitope of Plasmodium falciparum rhoptry associated protein 2 specifically raises antibodies to rhoptry associated protein 1. Molecular and Biochemical Parasitology 82(2): 167-180, 1996

Secretion of Plasmodium falciparum rhoptry protein into the plasma membrane of host erythrocytes. Journal of Cell Biology 106(5): 1507-1513, 1988