Antibodies to Reticulocyte Binding Protein-Like Homologue 4 Inhibit Invasion of Plasmodium falciparum into Human Erythrocytes Export

@article{citeulike:4746789, 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. 10.1128/IAI.00048-09}, author = {Tham, Wai-Hong and Wilson, Danny W. and Reiling, Linda and Chen, Lin and Beeson, James G. and Cowman, Alan F.}, citeulike-article-id = {4746789}, citeulike-linkout-0 = {http://dx.doi.org/10.1128/IAI.00048-09}, citeulike-linkout-1 = {http://iai.asm.org/cgi/content/abstract/77/6/2427}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/19307208}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=19307208}, day = {1}, doi = {10.1128/IAI.00048-09}, journal = {Infect. Immun.}, keywords = {antibody, malaria}, month = {June}, number = {6}, pages = {2427--2435}, posted-at = {2009-06-05 00:03:42}, priority = {2}, title = {Antibodies to Reticulocyte Binding Protein-Like Homologue 4 Inhibit Invasion of Plasmodium falciparum into Human Erythrocytes}, url = {http://dx.doi.org/10.1128/IAI.00048-09}, volume = {77}, year = {2009} }

TY - JOUR ID - citeulike:4746789 L3 - citeulike-article-id:4746789 N2 - 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. 10.1128/IAI.00048-09 IS - 6 JF - Infect. Immun. EP - 2435 TI - Antibodies to Reticulocyte Binding Protein-Like Homologue 4 Inhibit Invasion of Plasmodium falciparum into Human Erythrocytes VL - 77 SP - 2427 KW - antibody KW - malaria AU - Tham, Wai-Hong AU - Wilson, Danny AU - Reiling, Linda AU - Chen, Lin AU - Beeson, James AU - Cowman, Alan PY - 2009/06/01/ UR - http://dx.doi.org/10.1128/IAI.00048-09 ER -