Antibodies to Reticulocyte Binding Protein-Like Homologue 4 Inhibit Invasion of Plasmodium falciparum into Human Erythrocytes
- Author(s)
- Tham, WH; Wilson, DW; Reiling, L; Chen, L; Beeson, JG; Cowman, AF;
- Details
- Publication Year 2009-06,Volume 77,Issue #6,Page 2427-2435
- Journal Title
- INFECTION AND IMMUNITY
- Publication Type
- Journal Article
- Abstract
- Plasmodium falciparum invasion into human erythrocytes relies on the interaction between multiple parasite ligands and their respective erythrocyte receptors. The sialic acid-independent invasion pathway is dependent on the expression of P. falciparum reticulocyte binding protein-like homologue 4 (PfRh4), as disruption of the gene abolishes the ability of parasites to switch to this pathway. We show that PfRh4 is present as an invasion ligand in culture supernatants as a 160-kDa proteolytic fragment. We confirm that PfRh4 binds to the surfaces of erythrocytes through recognition of an erythrocyte receptor that is neuraminidase resistant but trypsin and chymotrypsin sensitive. Serum antibodies from malaria-exposed individuals show reactivity against the binding domain of PfRh4. Purified immunoglobulin G raised in rabbits against the binding domain of PfRh4 blocked the binding of native PfRh4 to the surfaces of erythrocytes and inhibited erythrocyte invasion of parasites using sialic acid-independent invasion pathways and grown in neuraminidase-treated erythrocytes. Our results suggest PfRh4 is a potential vaccine candidate.
- Publisher
- AMER SOC MICROBIOLOGY
- Keywords
- YOELII ADHESIVE PROTEINS; RED-BLOOD-CELL; MALARIA PARASITES; RECEPTOR HETEROGENEITY; MEROZOITE PROTEINS; GLYCOPHORIN-B; PATHWAYS; EBA-175; VIVAX; LIGAND
- Publisher's Version
- https://doi.org/10.1128/IAI.00048-09
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2009-06-01 12:00:00