Journal article

An egf-like protein forms a complex with pfrh5 and is required for invasion of human erythrocytes by plasmodium falciparum

L Chen, S Lopaticki, DT Riglar, C Dekiwadia, AD Uboldi, WH Tham, MT O'Neill, D Richard, J Baum, SA Ralph, AF Cowman

Plos Pathogens | Published : 2011

Abstract

Invasion of erythrocytes by Plasmodium falciparum involves a complex cascade of protein-protein interactions between parasite ligands and host receptors. The reticulocyte binding-like homologue (PfRh) protein family is involved in binding to and initiating entry of the invasive merozoite into erythrocytes. An important member of this family is PfRh5. Using ion-exchange chromatography, immunoprecipitation and mass spectroscopy, we have identified a novel cysteine-rich protein we have called P. falciparum Rh5 interacting protein (PfRipr) (PFC1045c), which forms a complex with PfRh5 in merozoites. Mature PfRipr has a molecular weight of 123 kDa with 10 epidermal growth factor-like domains and 8..

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Grants

Funding Acknowledgements

This work was supported by the National Health and Medical Research Council of Australia (NHMRC) (http://www.nhmrc.gov.au/), PATH Malaria Vaccine Initiative (http://www.malariavaccine.org/), Bill and Melinda Gates Foundation (http://www.gatesfoundation.org/). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.