Parasitology Research

, Volume 110, Issue 2, pp 545–556 | Cite as

Plasmodium falciparum infection-induced changes in erythrocyte membrane proteins

  • Albin Fontaine
  • Stéphanie Bourdon
  • Maya Belghazi
  • Mathieu Pophillat
  • Patrick Fourquet
  • Samuel Granjeaud
  • Marylin Torrentino-Madamet
  • Christophe Rogier
  • Thierry Fusai
  • Lionel Almeras
Original Paper


Over the past decade, advances in proteomic and mass spectrometry techniques and the sequencing of the Plasmodium falciparum genome have led to an increasing number of studies regarding the parasite proteome. However, these studies have focused principally on parasite protein expression, neglecting parasite-induced variations in the host proteome. Here, we investigated P. falciparum-induced modifications of the infected red blood cell (iRBC) membrane proteome, taking into account both host and parasite proteome alterations. Furthermore, we also determined if some protein changes were associated with genotypically distinct P. falciparum strains. Comparison of host membrane proteomes between iRBCs and uninfected red blood cells using fluorescence-based proteomic approaches, such as 2D difference gel electrophoresis revealed that more than 100 protein spots were highly up-represented (fold change increase greater than five) following P. falciparum infection for both strains (i.e. RP8 and Institut Pasteur Pregnancy Associated Malaria). The majority of spots identified by mass spectrometry corresponded to Homo sapiens proteins. However, infection-induced changes in host proteins did not appear to affect molecules located at the outer surface of the plasma membrane. The under-representation of parasite proteins could not be attributed to deficient parasite protein expression. Thus, this study describes for the first time that considerable host protein modifications were detected following P. falciparum infection at the erythrocyte membrane level. Further analysis of infection-induced host protein modifications will improve our knowledge of malaria pathogenesis.



This study was supported by Délégation Générale pour l’Armement (DGA, SalivaPuls Project grant nos. 07CO406 and 03CO008-05, ArthroSer Project grant no. 10Ca401). We thank Dr. Bruno Pouvelle for his useful discussion and his thoughtful comments and inputs.

Supplementary material

436_2011_2521_MOESM1_ESM.doc (64 kb)
Table S1P. falciparum proteins from iRBCs membrane extracts identified by LC Q-TOF. (DOC 64 kb)
436_2011_2521_MOESM2_ESM.doc (102 kb)
Table S2MS/MS.Human proteins from iRBCs membrane extracts identified by LC Q-TOF MS/MS. (DOC 102 kb)
436_2011_2521_MOESM3_ESM.doc (50 kb)
Table S3P. falciparum proteins from biotinylated iRBCs membrane extracts identified by LC Q-TOF MS/MS. (DOC 50 kb)
436_2011_2521_MOESM4_ESM.doc (40 kb)
Table S4Plasmodium falciparum proteins from iRBCs membrane extracts detected out of the master gel scope after metabolic labeling and identified by LC Q-TOF MS/MS. (DOC 39 kb)


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Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  • Albin Fontaine
    • 1
  • Stéphanie Bourdon
    • 1
  • Maya Belghazi
    • 2
  • Mathieu Pophillat
    • 3
  • Patrick Fourquet
    • 3
  • Samuel Granjeaud
    • 4
  • Marylin Torrentino-Madamet
    • 1
  • Christophe Rogier
    • 1
  • Thierry Fusai
    • 1
  • Lionel Almeras
    • 1
  1. 1.Unité de ParasitologieInstitut de Recherche Biomédicale des Armées (IRBA)Marseille Cedex 07France
  2. 2.Centre d’Analyse Proteomique de Marseille (CAPM)IFR Jean RocheMarseille cedex 20France
  3. 3.Centre d’Immunologie de Marseille Luminy (CIML), Institut National de la Santé et de la Recherche Médicale, Centre National de la Recherche ScientifiqueUniversité de la MéditerranéeMarseille Cedex 09France
  4. 4.TAGC INSERM ERM 206Marseille Cedex 9France

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