Localization, biosynthesis, processing and isolation of a major 126 kDa antigen of the parasitophorous vacuole of Plasmodium falciparum.

作者: Patrick Delplace , Bernard Fortier , Guy Tronchin , Jean-François Dubremetz , Alain Vernes

DOI: 10.1016/0166-6851(87)90026-0

关键词: Plasmodium falciparumRed blood cellPolyclonal antibodiesAntibodyImmunofluorescenceAntigenBiologyMonoclonal antibodyMolecular biologyBiochemistryPMSF

摘要: Monoclonal antibodies prepared against a 50 kDa antigen found in Plasmodium falciparum culture supernatants identify 126 polypeptide which can be localized by immunofluorescence and immunoelectronmicroscopy at the periphery of schizonts. This is released from infected erythrocytes mild saponin lysis probably component parasitophorous vacuole. Pulse chase kinetic analysis demonstrated its disappearance parasitized red blood cell 6 to 10 h after being synthesized concomitant appearance molecule supernatant. Purification metabolically labeled, schizont cells that spontaneous release merozoites needed for processing whereas reinvasion not. Polyclonal were raised rabbit affinity purified protein. These antibodies, together with another specific monoclonal antibody have enabled us characterize two other cleavage products supernatants, namely 47 18 polypeptides. We believe protein into low molecular weight fragments reflects proteolytic event may participate merozoite release.

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