1. Howard Hughes Medical Institute,
2. Departments of Genome Sciences and Medicine, University of Washington, Box 357730, Seattle, Washington 98195, USA
3. Prolexys Pharmaceuticals, Inc., 2150 West Dauntless Avenue, Salt Lake City, Utah 84111, USA
4. †Present address: Buck Institute, Novato, California 94945, USA
5. *These authors contributed equally to this work

Correspondence to: Stanley Fields^1,2Robert E. Hughes^3,4 Correspondence and requests for materials should be addressed to S.F. (Email: fields@u.washington.edu) or R.E.H. (Email: rhughes@buckinstitute.org).

Abstract

Plasmodium falciparum causes the most severe form of malaria and kills up to 2.7 million people annually¹. Despite the global importance of P. falciparum, the vast majority of its proteins have not been characterized experimentally. Here we identify P. falciparum protein–protein interactions using a high-throughput version of the yeast two-hybrid assay that circumvents the difficulties in expressing P. falciparum proteins in Saccharomyces cerevisiae. From more than 32,000 yeast two-hybrid screens with P. falciparum protein fragments, we identified 2,846 unique interactions, most of which include at least one previously uncharacterized protein. Informatic analyses of network connectivity, coexpression of the genes encoding interacting fragments, and enrichment of specific protein domains or Gene Ontology annotations² were used to identify groups of interacting proteins, including one implicated in chromatin modification, transcription, messenger RNA stability and ubiquitination, and another implicated in the invasion of host cells. These data constitute the first extensive description of the protein interaction network for this important human pathogen.

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