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  • The EMBO Journal (2005) 24, 2306 - 2317
  • doi:10.1038/sj.emboj.7600720

Published online: 16 June 2005

Trafficking of STEVOR to the Maurer's clefts in Plasmodium falciparum-infected erythrocytes

Jude M Przyborski1, Susanne K Miller2, Judith M Pfahler1, Philipp P Henrich1, Petra Rohrbach1, Brendan S Crabb2 and Michael Lanzer1

  1. Hygiene Institut, Abteilung Parasitologie, Universitätsklinikum Heidelberg, Heidelberg, Germany
  2. The Walter & Eliza Hall Institute of Medical Research, Parkville, VIC, Australia

Correspondence to:

Michael Lanzer, Hygiene Institut, Abteilung Parasitologie, Universitätsklinikum Heidelberg, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany. Tel.: +49 6221 567845; Fax: +49 6221 564643; E-mail: michael_lanzer@med.uni-heidelberg.de

Received 1 December 2004; Accepted 27 May 2005

The human malarial parasite Plasmodium falciparum exports proteins to destinations within its host erythrocyte, including cytosol, surface and membranous profiles of parasite origin termed Maurer's clefts. Although several of these exported proteins are determinants of pathology and virulence, the mechanisms and trafficking signals underpinning protein export are largely uncharacterized—particularly for exported transmembrane proteins. Here, we have investigated the signals mediating trafficking of STEVOR, a family of transmembrane proteins located at the Maurer's clefts and believed to play a role in antigenic variation. Our data show that, apart from a signal sequence, a minimum of two addition signals are required. This includes a host cell targeting signal for export to the host erythrocyte and a transmembrane domain for final sorting to Maurer's clefts. Biochemical studies indicate that STEVOR traverses the secretory pathway as an integral membrane protein. Our data suggest general principles for transport of transmembrane proteins to the Maurer's clefts and provide new insights into protein sorting and trafficking processes in P. falciparum.

  • Keywords:

    • malaria,
    • protein export,
    • trafficking signal,
    • transmembrane protein