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Molecular & Cellular Proteomics 4:582-593, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
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From the
Unité de Biologie des Interactions Hôte-Parasite, CNRS URA 2581, Institut Pasteur, 2528 Rue du Dr Roux, 75724 Paris Cedex 15, the ¶ Laboratoire de Spectrométrie de Masse Bio-Organique, 25 rue Becquerel, 67087 Strasbourg Cedex 2, the ** Laboratoire de Bioénergétique Cellulaire et Pathologique, Commissariat à lEnergie Atomique Grenoble, 17 rue des martyrs, 38054 Grenoble Cedex 9, and 
UMR 5539 CNRS-Université Montpellier 2, Place Eugène Bataillon, 34095 Montpellier Cedex 5, France
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 Maurers 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 Maurers 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 Maurers clefts was established for two of them. This suggests a clustering of genes encoding Maurers cleft proteins. Our study sheds new light on the biological function of the Maurers clefts, which are central to the pathogenesis and to the intraerythrocytic development of P. falciparum.

To whom correspondence should be addressed. Tel.: 33-4-67-14-33-81; Fax: 33-4-67-14-42-86; E-mail: cbb{at}univ-montp2.fr
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