title: Reticulocyte binding protein homologues are key adhesins during erythrocyte invasion by Plasmodium falciparum.
abstract: The Apicomplexan parasite responsible for the most virulent form of malaria, Plasmodium falciparum, invades human erythrocytes through multiple ligand-receptor interactions. The P. falciparum reticulocyte-binding protein homologue (PfRh or PfRBL) family have been implicated in the invasion process but their exact role is unknown. PfRh1 and PfRh4, members of this protein family, bind to red blood cells and function in merozoite invasion during which they undergo a series of proteolytic cleavage events before and during entry into the host cell. The ectodomain of PfRh1 and PfRh4 are processed to produce fragments consistent with cleavage in the transmembrane domain and released into the supernatant, at about the time of invasion, in a manner consistent with rhomboid protease cleavage. Processing of both PfRh1 and PfRh4, and by extrapolation all membrane-bound members of this protein family, is important for function and release of these proteins on the merozoite surface and they along with EBA-175 are important components of the tight junction, the transient structure that links the erythrocyte via receptor-ligand interactions to the actin-myosin motor in the invading merozoite.
authors.affiliation: The Walter and Eliza Hall Institute of Medical Research, Melbourne 3050, Australia.
authors.forename: Tony
authors.initials: T
authors.lastname: Triglia
authors.forename: Wai-Hong
authors.initials: WH
authors.lastname: Tham
authors.forename: Anthony
authors.initials: A
authors.lastname: Hodder
authors.forename: Alan F
authors.initials: AF
authors.lastname: Cowman
mesh_terms: D000818:Animals; D000953:Antigens, Protozoan / Q000502:physiology; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules / Q000502:physiology*; D004912:Erythrocytes / Q000469:parasitology*; D006801:Humans; D008565:Membrane Proteins / Q000502:physiology*; D008954:Models, Biological; D010963:Plasmodium falciparum / Q000472:pathogenicity*; D011499:Protein Processing, Post-Translational; D015800:Protozoan Proteins / Q000502:physiology*; D037521:Virulence Factors / Q000502:physiology*
chemical_list: D000953:Antigens, Protozoan; D015815:Cell Adhesion Molecules; D008565:Membrane Proteins; D015800:Protozoan Proteins; C503374:RH1 protein, Plasmodium falciparum; C464927:RH4 protein, Plasmodium falciparum; D037521:Virulence Factors; C065668:erythrocyte-binding antigen 175, Plasmodium