Abstract

Malaria is caused by parasites which live in host erythrocytes and remodel these cells to provide optimally for the parasites’ needs by exporting effector proteins into the host cells. Eight years ago the discovery of a host cell targeting sequence present in both soluble and transmembrane  P. falciparum  exported proteins generated a starting point for investigating the mechanism of parasite protein transport into infected erythrocytes. Since then many confusing facts about this targeting signal have emerged. In this paper, I try to make sense of them.

Highlights

  • Malaria is caused by parasites which live in host erythrocytes and remodel these cells to provide optimally for the parasites’ needs by exporting effector proteins into the host cells

  • Stuck in the protein translocation channel in the P. falciparum endoplasmic reticulum (ER) membrane, the protein export element (PEXEL) protein in transit is oriented such that the host cell targeting signal can bind PI3P at the cytoplasmic face of the ER membrane (Figure 2B, (2))

  • Delayed signal cleavage will lead to prolonged residence of the nascent PEXEL protein in the Sec61 channel, which in turn would allow interaction of the still cytosolic PEXEL signal with PI3P in the cytosolic leaflet of the ER membrane (Figure 2B)

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Summary

Introduction

Malaria is caused by parasites which live in host erythrocytes and remodel these cells to provide optimally for the parasites’ needs by exporting effector proteins into the host cells. Stuck in the protein translocation channel in the P. falciparum ER membrane, the PEXEL protein in transit is oriented such that the host cell targeting signal can bind PI3P at the cytoplasmic face of the ER membrane (Figure 2B, (2)).

Results
Conclusion
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