Spatial association with PTEX complexes defines regions for effector export into Plasmodium falciparum-infected erythrocytes

David T. Riglar, Kelly L. Rogers, Eric Hanssen, Lynne Turnbull, Hayley E. Bullen, Sarah C. Charnaud, Jude Przyborski, Paul R. Gilson, Cynthia B. Whitchurch, Brendan S. Crabb, Jake Baum () and Alan F. Cowman ()
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David T. Riglar: The Walter and Eliza Hall Institute of Medical Research
Kelly L. Rogers: The Walter and Eliza Hall Institute of Medical Research
Eric Hanssen: Electron Microscopy Unit, Bio21 Molecular Science and Biotechnology Institute
Lynne Turnbull: The ithree institute, University of Technology Sydney
Hayley E. Bullen: University of Melbourne
Sarah C. Charnaud: Macfarlane Burnet Institute for Medical Research and Public Health
Jude Przyborski: Philipps University Marburg
Paul R. Gilson: Macfarlane Burnet Institute for Medical Research and Public Health
Cynthia B. Whitchurch: The ithree institute, University of Technology Sydney
Brendan S. Crabb: Macfarlane Burnet Institute for Medical Research and Public Health
Jake Baum: The Walter and Eliza Hall Institute of Medical Research
Alan F. Cowman: The Walter and Eliza Hall Institute of Medical Research

Nature Communications, 2013, vol. 4, issue 1, 1-13

Abstract: Abstract Export of proteins into the infected erythrocyte is critical for malaria parasite survival. The majority of effector proteins are thought to export via a proteinaceous translocon, resident in the parasitophorous vacuole membrane surrounding the parasite. Identification of the Plasmodium translocon of exported proteins and its biochemical association with exported proteins suggests it performs this role. Direct evidence for this, however, is lacking. Here using viable purified Plasmodium falciparum merozoites and three-dimensional structured illumination microscopy, we investigate remodelling events immediately following parasite invasion. We show that multiple complexes of the Plasmodium translocon of exported proteins localize together in foci that dynamically change in clustering behaviour. Furthermore, we provide conclusive evidence of spatial association between exported proteins and exported protein 2, a core component of the Plasmodium translocon of exported proteins, during native conditions and upon generation of translocation intermediates. These data provide the most direct cellular evidence to date that protein export occurs at regions of the parasitophorous vacuole membrane housing the Plasmodium translocon of exported proteins complex.

Date: 2013
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2449

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DOI: 10.1038/ncomms2449

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