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Proteomic analysis identifies novel proteins of the Maurer's clefts, a secretory compartment delivering Plasmodium falciparum proteins to the surface of its host cell
Authors:Vincensini Laetitia  Richert Sophie  Blisnick Thierry  Van Dorsselaer Alain  Leize-Wagner Emmanuelle  Rabilloud Thierry  Braun Breton Catherine
Institution:3. Unité de Biologie des Interactions Hôte-Parasite, CNRS URA 2581, Institut Pasteur, 25–28 Rue du Dr Roux, 75724 Paris Cedex 15;5. Laboratoire de Spectrométrie de Masse Bio-Organique, 25 rue Becquerel, 67087 Strasbourg Cedex 2;12. UMR 5539 CNRS-Université Montpellier 2, Place Eugène Bataillon, 34095 Montpellier Cedex 5, France
Abstract:A novel method was validated for the efficient distinction between malaria parasite-derived and host cell proteins in mass spectrometry analyses. This method was applied to a ghost fraction from Plasmodium falciparum-infected erythrocytes containing the red blood cell plasma membrane, the erythrocyte submembrane skeleton, and the Maurer's clefts, a Golgi-like apparatus linked to and addressing parasite proteins to the host cell surface. This method allowed the identification of 78 parasite proteins. Among these we identified seven novel proteins of the Maurer's clefts based on immunofluorescence studies and proteinase K digestion assays. The products of six contiguous genes located on chromosome 5 were identified, and the location within the Maurer's clefts was established for two of them. This suggests a clustering of genes encoding Maurer's cleft proteins. Our study sheds new light on the biological function of the Maurer's clefts, which are central to the pathogenesis and to the intraerythrocytic development of P. falciparum.
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