Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum
Article first published online: 24 NOV 2008
© 2008 The Authors. Journal compilation © 2008 Blackwell Publishing Ltd
Volume 71, Issue 3, pages 613–628, February 2009
How to Cite
Gehde, N., Hinrichs, C., Montilla, I., Charpian, S., Lingelbach, K. and Przyborski, J. M. (2009), Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum. Molecular Microbiology, 71: 613–628. doi: 10.1111/j.1365-2958.2008.06552.x
- Issue published online: 14 JAN 2009
- Article first published online: 24 NOV 2008
- Accepted 12 November, 2008.
Plasmodium falciparum traffics a large number of proteins to its host cell, the mature human erythrocyte. How exactly these proteins gain access to the red blood cell is poorly understood. Here we have investigated the effect of protein folding on the transport of model substrate proteins to the host cell. We find that proteins must pass into the erythrocyte cytoplasm in an unfolded state. Our data strongly support the presence of a protein-conducing channel in the parasitophorous vacoular membrane, and additionally imply an important role for molecular chaperones in keeping parasite proteins in a ‘translocation competent’ state prior to membrane passage.