A protein interaction network of the malaria parasite Plasmodium falciparum

Douglas J. LaCount, Marissa Vignali, Rakesh Chettier, Amit Phansalkar, Russell Bell, Jay R. Hesselberth, Lori W. Schoenfeld, Irene Ota, Sudhir Sahasrabudhe, Cornelia Kurschner, Stanley Fields () and Robert E. Hughes ()
Additional contact information
Douglas J. LaCount: Howard Hughes Medical Institute
Marissa Vignali: University of Washington
Rakesh Chettier: Prolexys Pharmaceuticals, Inc.
Amit Phansalkar: Prolexys Pharmaceuticals, Inc.
Russell Bell: Prolexys Pharmaceuticals, Inc.
Jay R. Hesselberth: University of Washington
Lori W. Schoenfeld: Howard Hughes Medical Institute
Irene Ota: Prolexys Pharmaceuticals, Inc.
Sudhir Sahasrabudhe: Prolexys Pharmaceuticals, Inc.
Cornelia Kurschner: Prolexys Pharmaceuticals, Inc.
Stanley Fields: Howard Hughes Medical Institute
Robert E. Hughes: Prolexys Pharmaceuticals, Inc.

Nature, 2005, vol. 438, issue 7064, 103-107

Abstract: What makes a parasite tick A powerful approach for understanding protein function is to identify which proteins bind to each other, as protein complexes are at the heart of most biological processes. Protein–protein interactions have now been mapped for one quarter of the malaria parasite's proteins. This large data set sheds new light on how parasites infect red blood cells and will be a vital tool for the development of new antimalarial drugs and vaccines. The primary data are freely available on the PlasmoDB database. Suthram et al. have used this new resource and find that the Plasmodium network has significantly less cross-species similarity than other eukaryotes. Its novel life style is reflected in a novel protein network, which therefore has a good chance of providing drug targets unique to the malaria parasite.

Date: 2005
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DOI: 10.1038/nature04104

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