Openly accessible

An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytes

Batinovic, Steven, McHugh, Emma, Chisholm, Scott A., Matthews, Kathryn, Liu, Boiyin, Dumont, Laure, Charnaud, Sarah C., Parkyn Schneider, Molly, Gilson, Paul R., De Koning-Ward, Tania F., Dixon, Matthew W. A. and Tilley, Leann 2017, An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytes, Nature communications, vol. 8, pp. 1-14, doi: 10.1038/ncomms16044.

Attached Files
Name Description MIMEType Size Downloads
chisholm-anexportedprotein-2017.pdf Published version application/pdf 2.81MB 102

Title An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytes
Author(s) Batinovic, Steven
McHugh, Emma
Chisholm, Scott A.
Matthews, Kathryn
Liu, Boiyin
Dumont, Laure
Charnaud, Sarah C.
Parkyn Schneider, Molly
Gilson, Paul R.
De Koning-Ward, Tania F.ORCID iD for De Koning-Ward, Tania F. orcid.org/0000-0001-5810-8063
Dixon, Matthew W. A.
Tilley, Leann
Journal name Nature communications
Volume number 8
Article ID 16044
Start page 1
End page 14
Total pages 14
Publisher Nature Publishing Group
Place of publication London, Eng.
Publication date 2017-07-10
ISSN 2041-1723
Keyword(s) Science & Technology
Multidisciplinary Sciences
Science & Technology - Other Topics
Summary The malaria parasite, Plasmodium falciparum, displays the P. falciparum erythrocyte membrane protein 1 (PfEMP1) on the surface of infected red blood cells (RBCs). We here examine the physical organization of PfEMP1 trafficking intermediates in infected RBCs and determine interacting partners using an epitope-tagged minimal construct (PfEMP1B). We show that parasitophorous vacuole (PV)-located PfEMP1B interacts with components of the PTEX (Plasmodium Translocon of EXported proteins) as well as a novel protein complex, EPIC (Exported Protein-Interacting Complex). Within the RBC cytoplasm PfEMP1B interacts with components of the Maurer's clefts and the RBC chaperonin complex. We define the EPIC interactome and, using an inducible knockdown approach, show that depletion of one of its components, the parasitophorous vacuolar protein-1 (PV1), results in altered knob morphology, reduced cell rigidity and decreased binding to CD36. Accordingly, we show that deletion of the Plasmodium berghei homologue of PV1 is associated with attenuation of parasite virulence in vivo.
Language eng
DOI 10.1038/ncomms16044
Field of Research 110309 Infectious Diseases
060108 Protein Trafficking
060599 Microbiology not elsewhere classified
MD Multidisciplinary
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Grant ID NHMRC 1078065
Copyright notice ©2017, The Authors
Free to Read? Yes
Use Rights Creative Commons Attribution licence
Persistent URL http://hdl.handle.net/10536/DRO/DU:30097884

Document type: Journal Article
Collections: Faculty of Health
School of Medicine
Open Access Collection
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 24 times in TR Web of Science
Scopus Citation Count Cited 24 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 357 Abstract Views, 103 File Downloads  -  Detailed Statistics
Created: Mon, 17 Jul 2017, 11:23:01 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.