Open AccessSpatial and temporal mapping of the PfEMP1 export pathway in P lasmodium falciparum
Author(s) -
McMillan Paul J.,
Millet Coralie,
Batinovic Steven,
Maiorca Mauro,
Hanssen Eric,
Kenny Shan,
Muhle Rebecca A.,
Melcher Martin,
Fidock David A.,
Smith Joseph D.,
Dixon Matthew W. A.,
Tilley Leann
Publication year - 2013
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/cmi.12125
Subject(s) - plasmodium falciparum , biology , microbiology and biotechnology , ultrastructure , green fluorescent protein , cytochalasin d , transport protein , transmembrane protein , membrane protein , vesicle , transfection , cytoskeleton , membrane , cell , receptor , anatomy , gene , biochemistry , malaria , immunology
Summary The human malaria parasite, P lasmodium falciparum , modifies the red blood cells ( RBCs ) that it infects by exporting proteins to the host cell. One key virulence protein, P . falciparum E rythrocyte M embrane P rotein‐1 ( PfEMP1 ), is trafficked to the surface of the infected RBC , where it mediates adhesion to the vascular endothelium. We have investigated the organization and development of the exomembrane system that is used for PfEMP1 trafficking. M aurer's cleft cisternae are formed early after invasion and proteins are delivered to these (initially mobile) structures in a temporally staggered and spatially segregated manner. M embrane‐ A ssociated H istidine‐ R ich P rotein‐2( MAHRP2 )‐containing tether‐like structures are generated as early as 4 h post invasion and become attached to M aurer's clefts. The tether/ M aurer's cleft complex docks onto the RBC membrane at ∼ 20 h post invasion via a process that is not affected by cytochalasin D treatment. We have examined the trafficking of a GFP chimera of PfEMP1 expressed in transfected parasites. PfEMP1B ‐ GFP accumulates near the parasite surface, within membranous structures exhibiting a defined ultrastructure, before being transferred to pre‐formed mobile M aurer's clefts. Endogenous PfEMP1 and PfEMP1B ‐ GFP are associated with E lectron‐ D ense V esicles that may be responsible for trafficking PfEMP1 from the M aurer's clefts to the RBC membrane.