title: Pfsbp1, a Maurer's cleft Plasmodium falciparum protein, is associated with the erythrocyte skeleton.
abstract: Antibodies from hyperimmune monkey sera, selected by absorption to Plasmodium falciparum-infected erythrocytes, and elution at acidic pH, allowed us to characterize a novel parasite protein, Pfsbp1 (P. falciparum skeleton binding protein 1). Pfsbp1 is an integral membrane protein of parasite-induced membranous structures associated with the erythrocyte plasma membrane and referred to as Maurer's clefts. The carboxy-terminal domain of Pfsbp1, exposed within the cytoplasm of the host cell, interacts with a 35 kDa erythrocyte skeletal protein and might participate in the binding of the Maurer's clefts to the erythrocyte submembrane skeleton. Antibodies to the carboxy- and amino-terminal domains of Pfsbp1 labelled similar vesicular structures in the cytoplasm of Plasmodium chabaudi and Plasmodium berghei-infected murine erythrocytes, suggesting that the protein is conserved among malaria species, consistent with an important role of Maurer's cleft-like structures in the intraerythrocytic development of malaria parasites.
authors.affiliation: Unité de Biologie des Interactions Hôte-Parasite, Institut Pasteur, 25 Rue du Dr. Roux, Paris 75015, France.
authors.forename: T
authors.initials: T
authors.lastname: Blisnick
authors.forename: M E
authors.initials: ME
authors.lastname: Morales Betoulle
authors.forename: J C
authors.initials: JC
authors.lastname: Barale
authors.forename: P
authors.initials: P
authors.lastname: Uzureau
authors.forename: L
authors.initials: L
authors.lastname: Berry
authors.forename: S
authors.initials: S
authors.lastname: Desroses
authors.forename: H
authors.initials: H
authors.lastname: Fujioka
authors.forename: D
authors.initials: D
authors.lastname: Mattei
authors.forename: C
authors.initials: C
authors.lastname: Braun Breton
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001798:Blood Proteins / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D002846:Chromatography, Affinity; D003001:Cloning, Molecular; D022162:Cytoplasmic Vesicles / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000469:parasitology*; D018628:Gene Dosage; D017125:Genes, Protozoan; D008288:Malaria / Q000469:parasitology; D016778:Malaria, Falciparum / Q000469:parasitology; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000235:genetics / Q000378:metabolism*; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012453:Saimiri
chemical_list: D001798:Blood Proteins; D002352:Carrier Proteins; D008565:Membrane Proteins; C417763:Pfsbp1 protein, Plasmodium falciparum; D015800:Protozoan Proteins; D011993:Recombinant Fusion Proteins