Plasmodium falciparum: Molecular analysis of a putative protective antigen, the thermostable 96-kDa protein

Bonnefoy, Serge; Mattei, Denise; Dubremetz, Jean‐François; Guillotte, Micheline; Jouin, H; Ozaki, Luiz Shozo; Sibilli, Lise; Mercereau‐Puijalon, Odile

doi:10.1016/0014-4894(88)90108-7

Cited by 33 publications

(13 citation statements)

References 26 publications

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“…Three proteins reported to be exported to the host erythrocyte, GBP130, Stevor and RESA, were recovered in this analysis. GBP130 is abundant in the erythrocyte cytoplasm [49]. Hence, it can be taken up together with Hb during the parasite feeding process.…”

Section: Parasite Surface Proteinsmentioning

confidence: 99%

Food vacuole proteome of the malarial parasite Plasmodium falciparum

Lamarque

Tastet

Poncet

et al. 2008

Proteomics Clinical Apps

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The Plasmodium falciparum food vacuole (FV) is a lysosome-like organelle where erythrocyte hemoglobin digestion occurs. It is a favorite target in the development of antimalarials. We have used a tandem mass spectrometry approach to investigate the proteome of an FV-enriched fraction and identified 116 proteins. The electron microscopy analysis and the Western blot data showed that the major component of the fraction was the FV and, as expected, the majority of previously known FV markers were recovered. Of particular interest, several proteins involved in vesicle-mediated trafficking were identified, which are likely to play a key role in FV biogenesis and/or FV protein trafficking. Recovery of parasite surface proteins lends support to the cytostomal pathway of hemoglobin ingestion as a FV trafficking route. We have identified 32 proteins described as hypothetical in the databases. This insight into FV protein content provides new clues towards understanding the biological function of this organelle in P. falciparum.

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Section: Parasite Surface Proteinsmentioning

confidence: 99%

Food vacuole proteome of the malarial parasite Plasmodium falciparum

Lamarque

Tastet

Poncet

et al. 2008

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“…p126 processing was observed, but the inhibitors were reported to have a deleterious effect on the parasites. The proteases involved in the processing of the GBP 130 into 100,000 and 80,000 subfragments [11,59], or of the rhoptry antigens have not yet been characterised [12].…”

Section: Effects Of Protease Inhibitors On the Processing Of Major Pamentioning

confidence: 99%

Neutral proteases involved in the reinvasion of erythrocytes by Plasmodium merozoites

Schrével

Grellier

Mayer

et al. 1988

Biology of the Cell

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Neutral proteases of Plasmodium sp erythrocytic stages were studied by means of a sensitive fluorogenic method and gelatin-SDS-PAGE. The substrates gluconoyl-Val-Leu-Gly-Lys(or Arg)-3-amido-9-ethylcarbazole were selectively hydrolyzed by an endopeptidase from rodent Plasmodium berghei (Pb) and Plasmodium chabaudi (Pc) and from human Plasmodium falciparum (Pf) parasites. These endopeptidases were purified from 100,000-g soluble schizont extract by high pressure liquid chromatography; they have a similar Mr of 68,000 in SDS-PAGE, and an optimal activity at pH 7.4. The Pb 68 and Pf 68 endopeptidases were localized in schizonts and also in merozoites as shown by indirect immunofluorescence on Pb merozoites and by the identification of the Pf 68 endopeptidase activity in free viable merozoites. The Pb 68 and Pf 68 endopeptidases belong to the class of cysteine proteases. Analysis by gelatin-SDS-PAGE of a Pb 68 endopeptidase-enriched fraction showed a reproducible 95,000 proteolytic band. The initial extracts showed a similar 95,000 proteolytic band, and also 2 other 90,000 and 85,000 major bands. During reinvasion experiments, it was possible to recover a 95,000 and a 40,000 protease band from supernates of cultures grown in a semidefined medium without serum. Hydrophilic peptide derivatives related to the substrate of Pf 68 endopeptidase are shown to be potential inhibitors of the Pf reinvasion process in vitro.

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“…Processing of the major surface antigen p190, the glycophorin binding protein GBP 130, and the p126 protein seem to be concomitant with schizont rupture and merozoite release. GBP 130 is synthesized by trophozoites and accumulates at the schizont stage [8,46]; it is processed to a triplet of 3 polypeptides (pl30, pl00, and p80), which are recovered in merozoite preparations [46]. These proteins are removed from merozoites by washing, which indicates a loose association with the parasite surface.…”

Section: Introductionmentioning

confidence: 99%

Activation of a Plasmodium falciparum protease correlated with merozoite maturation and erythrocyte invasion

Braun-Breton

Silva

1988

Biology of the Cell

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Protease-dependent processes of the P. falciparum schizogonic cycle are briefly described. The P. falciparum p76 protease is the first example of a biochemically regulated protease, the activation of which is related to merozoite maturation and/or erythrocyte invasion. The main known properties of the p76 protease are reviewed and some original results concerning its biosynthesis and biological properties are described.

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Plasmodium falciparum: Molecular analysis of a putative protective antigen, the thermostable 96-kDa protein

Cited by 33 publications

References 26 publications

Food vacuole proteome of the malarial parasite Plasmodium falciparum

Food vacuole proteome of the malarial parasite Plasmodium falciparum

Neutral proteases involved in the reinvasion of erythrocytes by Plasmodium merozoites

Activation of a Plasmodium falciparum protease correlated with merozoite maturation and erythrocyte invasion

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