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Organization of ETRAMPs and EXP‐1 at the parasite–host cell interface of malaria parasites
Author(s) -
Spielmann Tobias,
Gardiner Donald L.,
Beck HansPeter,
Trenholme Katharine R.,
Kemp David J.
Publication year - 2006
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2005.04983.x
Subject(s) - biology , parasite hosting , plasmodium falciparum , microbiology and biotechnology , intracellular parasite , membrane protein , host (biology) , compartment (ship) , integral membrane protein , cell membrane , malaria , intracellular , membrane , biochemistry , genetics , immunology , oceanography , geology , world wide web , computer science
Summary The parasite–host cell interface is a key compartment of vacuolated intracellular pathogens but little is known about its molecular composition and architecture. We used in vivo cross‐linking to analyse the parasite–host cell interface of asexual stages of the most virulent human malaria parasite Plasmodium falciparum . We show that the integral membrane protein members of the early transcribed membrane protein (ETRAMP) family and exported protein 1 (EXP‐1), which are components of the parasite–host cell interface, form complexes of oligomeric arrays in this compartment. The most notable feature is that each ETRAMP member and EXP‐1 define separate arrays, demonstrating that the protein distribution in this membrane is non‐random. Each of three recombinant ETRAMPs readily oligomerized in bacterial membranes, confirming that these arrays can form independently of other Plasmodium proteins. We propose that the malaria parasite–host cell interface contains patches of integral membrane proteins forming a mosaic of different microdomains in this membrane.