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Food vacuole proteome of the malarial parasite Plasmodium falciparum
Author(s) -
Lamarque Mauld,
Tastet Christophe,
Poncet Joël,
Demettre Edith,
Jouin Patrick,
Vial Henri,
Dubremetz JeanFrançois
Publication year - 2008
Publication title -
proteomics – clinical applications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.948
H-Index - 54
eISSN - 1862-8354
pISSN - 1862-8346
DOI - 10.1002/prca.200700112
Subject(s) - proteome , vacuole , biogenesis , organelle , plasmodium falciparum , biology , western blot , microbiology and biotechnology , parasite hosting , lysosome , biochemistry , malaria , enzyme , immunology , gene , cytoplasm , world wide web , computer science
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 .