Document Detail


Evidence for vesicle-mediated trafficking of parasite proteins to the host cell cytosol and erythrocyte surface membrane in Plasmodium falciparum infected erythrocytes.
MedLine Citation:
PMID:  10743617     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Plasmodium falciparum malaria parasites actively remodel the host cell cytosol and plasma membrane during the erythrocytic cycle. The focus of this investigation was to characterize intra-parasitic and -erythrocytic secretory pathways. Electron-dense vesicles, similar in appearance to mammalian secretory vesicles were detected in proximity to smooth tubo-vesicular elements at the periphery of the parasite cytoplasm in mature parasites by transmission electron microscopy. Vesicles (60-100 nm diameter), which appeared to be coated, were visualized on the erythrocytic side of the parasite vacuolar membrane and in the erythrocyte cytosol. The vesicles seemed to bind to and fuse with the erythrocyte membrane, giving rise to cup-shaped electron-dense structures, which might be intermediates in knob structure formation. Treatment of mature parasites with aluminum tetrafluoride, an activator of GTP-binding proteins, resulted in the accumulation of the vesicles with an electron-dense limiting membrane in the erythrocyte cytosol into multiple vesicle strings. These vesicle complexes were often associated with and closely abutted the erythrocyte membrane, but were apparently prevented from fusing by the aluminum fluoride treatment. The parasite proteins PfEMP1 and PfEMP3 were found by immunoelectron microscopy to be associated with these vesicles, suggesting they are responsible for transporting these proteins to the erythrocyte membrane.
Authors:
D P Trelka; T G Schneider; J C Reeder; T F Taraschi
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular and biochemical parasitology     Volume:  106     ISSN:  0166-6851     ISO Abbreviation:  Mol. Biochem. Parasitol.     Publication Date:  2000 Feb 
Date Detail:
Created Date:  2000-05-10     Completed Date:  2000-05-10     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8006324     Medline TA:  Mol Biochem Parasitol     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  131-45     Citation Subset:  IM    
Affiliation:
Department of Pathology, Anatomy and Cell Biology, Jefferson Medical College, Philadelphia, PA 19107, USA.
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MeSH Terms
Descriptor/Qualifier:
Aluminum Compounds / pharmacology
Animals
Cytosol / metabolism,  parasitology
Erythrocyte Membrane / metabolism,  parasitology
Erythrocytes / metabolism,  parasitology*,  ultrastructure
Fluorides / pharmacology
Humans
Immunohistochemistry
Membrane Proteins / analysis,  metabolism
Microscopy, Electron
Plasmodium falciparum / drug effects,  metabolism*,  ultrastructure
Protozoan Proteins / analysis,  metabolism*
Grant Support
ID/Acronym/Agency:
AI41761/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Aluminum Compounds; 0/Fluorides; 0/Membrane Proteins; 0/Protozoan Proteins; 0/erythrocyte membrane protein 1, Plasmodium falciparum; 21340-02-3/tetrafluoroaluminate

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