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Trafficking and assembly of the cytoadherence complex in Plasmodium falciparum ‐infected human erythrocytes
Author(s) -
Wickham Mark E.,
Rug Melanie,
Ralph Stuart A.,
Klonis Nectarios,
McFadden Geoffrey I.,
Tilley Leann,
Cowman Alan F.
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.20.5636
Subject(s) - biology , plasmodium falciparum , endomembrane system , parasite hosting , cytoplasm , fluorescence recovery after photobleaching , microbiology and biotechnology , plasmodium (life cycle) , glycoprotein , golgi apparatus , malaria , virology , biochemistry , endoplasmic reticulum , immunology , membrane , world wide web , computer science
After invading human erythrocytes, the malarial parasite Plasmodium falciparum , initiates a remarkable process of secreting proteins into the surrounding erythrocyte cytoplasm and plasma membrane. One of these exported proteins, the knob‐associated histidine‐rich protein (KAHRP), is essential for microvascular sequestration, a strategy whereby infected red cells adhere via knob structures to capillary walls and thus avoid being eliminated by the spleen. This cytoadherence is an important factor in many of the deaths caused by malaria. Green fluorescent protein fusions and fluorescence recovery after photobleaching were used to follow the pathway of KAHRP deployment from the parasite endomembrane system into an intermediate depot between parasite and host, then onwards to the erythrocyte cytoplasm and eventually into knobs. Sequence elements essential to individual steps in the pathway are defined and we show that parasite‐derived structures, known as Maurer's clefts, are an elaboration of the canonical secretory pathway that is transposed outside the parasite into the host cell, the first example of its kind in eukaryotic biology.