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Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum
Author(s) -
Gehde Nina,
Hinrichs Corinna,
Montilla Irine,
Charpian Stefan,
Lingelbach Klaus,
Przyborski Jude M.
Publication year - 2009
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2008.06552.x
Subject(s) - biology , cytoplasm , plasmodium falciparum , microbiology and biotechnology , membrane protein , transport protein , protein folding , red blood cell , membrane , biochemistry , malaria , immunology
Summary 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.