MOLECULAR BIOCHEMICAL PARASITOLOGY zyxwvu ELSEVIER Molecular and Biochemical Parasitology 70 (1995) 235-239 Short communication The primary structure of a putative phosphatidylethanolamine-binding protein from zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCB Plasmodium falciparum Fraqois Trottein I, Alan F. Cowman * The W alter and Eliza Hall Institute of Medical Research, Post Ofice, Royal Melbourne Hospital, Victoria 3050. Australia Received 13 October 1994; accepted 16 January 1995 Keywords: Plasmodium falciparum; Phospholipid-transfer protein; Phosphatidylethanolamine-binding protein; Molecular cloning; lntergenic region The phospholipid-transfer proteins (PLTPs) are a family of ubiquitous and multifunctional intracellular transporters that are implicated in translocation of phospholipids between their site of synthesis to cell membranes [l]. They have a pivotal role in phospho- lipid metabolism, in membrane biogenesis and in the maintenance of membrane lipid composition and flu- idity [2]. Other cellular functions are also suspected including a role in protein secretion by the mem- brane vesicle flow phenomenon [3]. PLTPs act as carriers of phospholipids and include the phos- Abbreviations: PLTP, Phospholipid-transfer protein; PE-BP, Phosphatidylethanolamine-binding protein; PfPE-BPl, PE-BP from Plasmodium falciparum; PWI’Pase, P-type ATPase from P. falciparum. Note: Nucleotide sequence data reported in this paper have been submitted to the Genbank” data base with the accession number U18984. * Corresponding author. Tel.: (61-3) 345-2446; Fax: (61-3) 347-0852. ’ Present address: Centre d’Immunologie et de Biologie Para- sitaire, Institut Pasteur de Lille, 1 rue du Professeur Calmette, 59019 Lille Ctdex, France. phatidylcholine transfer protein [4], the phos- phatidylinositol transfer protein [5], and the non- specific lipid transfer protein [6]. Although its lipid transfer activity has not been clearly established, the phosphatidylethanolamine-binding protein (PE-BP) is probably a member of the PLTP family [7]. In mammals, the PE-BPS are found in many tissues in a cytosolic form [7], but they also exist in a membrane-bound form [8] or in secretion fluids [9]. They have a molecular mass ranging from 21 to 23 kDa and possess a PE-saturable binding site. Little is known about their three-dimensional structure and the amino acids involved in the lipid interaction. In this paper we report the molecular cloning of a putative member of the PE-BP family from zyxwvutsrqpo Plus- modium falciparum. The gene we have identified (PfPE-BPl), encodes a protein which shares both structural features and sequence homology with the PE-BPS from higher and lower eukaryotes. We have also identified two regions of the molecule which may be essential for the biological activity of the PE-BP family. The PfPE-BP1 gene is located about .500-bp up- 0166-6851/95/%09.50 0 1995 Elsevier Science B.V. All rights reserved XSDI 0166-6851(95)00031-3