title: Organization of ETRAMPs and EXP-1 at the parasite-host cell interface of malaria parasites.
abstract: 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.
authors.affiliation: Infectious Diseases and Immunology Division, Queensland Institute of Medical Research, PO Royal Brisbane Hospital, QLD 4029, Australia. tobiasS@qimr.edu.au
authors.forename: Tobias
authors.initials: T
authors.lastname: Spielmann
authors.forename: Donald L
authors.initials: DL
authors.lastname: Gardiner
authors.forename: Hans-Peter
authors.initials: HP
authors.lastname: Beck
authors.forename: Katharine R
authors.initials: KR
authors.lastname: Trenholme
authors.forename: David J
authors.initials: DJ
authors.lastname: Kemp
mesh_terms: D000818:Animals; D000953:Antigens, Protozoan / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000737:chemistry; D004912:Erythrocytes / Q000737:chemistry / Q000378:metabolism / Q000469:parasitology*; D006790:Host-Parasite Interactions; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D010963:Plasmodium falciparum / Q000187:drug effects / Q000378:metabolism / Q000472:pathogenicity*; D015800:Protozoan Proteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic
chemical_list: D000953:Antigens, Protozoan; D003432:Cross-Linking Reagents; D008565:Membrane Proteins; D015800:Protozoan Proteins; C063362:QF116 antigen, Plasmodium falciparum