Dissemin is shutting down on January 1st, 2025

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Elsevier, Molecular and Biochemical Parasitology, 2(67), p. 235-243

DOI: 10.1016/0166-6851(94)00136-7

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Photoaffinity labelling of Plasmodium falciparum proteins involved in phospholipid transport

This paper is available in a repository.
This paper is available in a repository.

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Abstract

Erythrocytes infected with mature-stage malaria parasites accumulate phospholipids from exogenous sources. We show that the transport of N-(7-nitrobenzy-2-oxa-1,3-diazol-4-yl)-1,2- ipalmitoyl-sn-glycero-3-phosphatidylethanolamine (N NBD-DPPE), from the erythrocyte membrane to the intracellular malaria parasite, is dependent upon metabolic energy, A photoreactive phospholipid analogue, N-[125I]iodo-4-azidosalicylamidy1-1,2-dilaury1-sn-glycero-3-phosphatidylethanolamine (N-125I-ASA-DLPE), has been synthesised and used in an attempt to identify proteins involved in phospholipid trafficking in malaria-infected erythrocytes. This photoreactive probe was found to preferentially label a protein with an apparent molecular weight of 22 kDa. Photolabelling of the 22-kDa protein was enhanced upon ATP depletion of malaria-infected erythrocytes.