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Characterization of membrane proteins exported from Plasmodium falciparum into the host erythrocyte

Published online by Cambridge University Press:  06 April 2009

D. Johnson ,
K. Günther ,
I. Ansorge ,
J. Benting ,
A. Kent ,
L. Bannister ,
R. Ridley  and
K. Lingelbach
D. Johnson
Affiliation:
Department of Molecular Biology, University of Edinburgh, King's Buildings, Edinburgh, UK
K. Günther
Affiliation:
Bernhard Nocht Institute for Tropical Medicine, Hamburg, FRG
I. Ansorge
Affiliation:
Bernhard Nocht Institute for Tropical Medicine, Hamburg, FRG
J. Benting
Affiliation:
Bernhard Nocht Institute for Tropical Medicine, Hamburg, FRG
A. Kent
Affiliation:
Department of Anatomy and Cell Biology, Guy's Hospital Medical School, London, UK
L. Bannister
Affiliation:
Department of Anatomy and Cell Biology, Guy's Hospital Medical School, London, UK
R. Ridley
Affiliation:
Department of Molecular Biology, University of Edinburgh, King's Buildings, Edinburgh, UK
K. Lingelbach
Affiliation:
Bernhard Nocht Institute for Tropical Medicine, Hamburg, FRG
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Summary

Plasmodium falciparum is an intracellular parasite of the red blood cell. During development it exports proteins which are transported to specific locations within the host erythrocyte. We have begun to identify and characterize exported membrane proteins of P.falciparum in order to obtain specific marker molecules for the study of the mechanisms involved in the distribution of parasite-derived proteins within the host cell. In this report we describe the characterization of a 35 kDa protein which is recognized by a monoclonal antibody. The protein is tightly associated with membranes isolated from infected erythrocytes; it is resistant to extraction with alkali and soluble after treatment with detergents. It is located at the membrane of the parasitophorous vacuole and in membrane-bound compartments which appear in the cytoplasm of the infected erythrocyte. The protein co-localizes with the previously described exported protein-1 (exp-1). Considering its localization and physical similarities to exp-1, we name the 35 kDa protein the exported protein-2 (exp-2).

Keywords

Plasmodium falciparummembrane proteinparasitophorous vacuoleprotein transport
Type
Research Article
Information
Parasitology , Volume 109 , Issue 1 , July 1994 , pp. 1 - 9
Copyright
Copyright © Cambridge University Press 1994

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