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Proteomic analysis reveals novel proteins associated with the Plasmodium protein exporter PTEX and a loss of complex stability upon truncation of the core PTEX component, PTEX150

Elsworth, Brendan, Sanders, Paul R., Nebl, Thomas, Batinovic, Steven, Kalanon, Ming, Nie, Catherine Q., Charnaud, Sarah C., Bullen, Hayley E., de Koning-Ward, Tania F., Tilley, Leann, Crabb, Brendan S. and Gilson, Paul R. 2016, Proteomic analysis reveals novel proteins associated with the Plasmodium protein exporter PTEX and a loss of complex stability upon truncation of the core PTEX component, PTEX150, Cell Microbiology, vol. 18, no. 11, pp. 1551-1569, doi: 10.1111/cmi.12596.

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Title Proteomic analysis reveals novel proteins associated with the Plasmodium protein exporter PTEX and a loss of complex stability upon truncation of the core PTEX component, PTEX150
Author(s) Elsworth, Brendan
Sanders, Paul R.
Nebl, Thomas
Batinovic, Steven
Kalanon, Ming
Nie, Catherine Q.
Charnaud, Sarah C.
Bullen, Hayley E.
de Koning-Ward, Tania F.ORCID iD for de Koning-Ward, Tania F. orcid.org/0000-0001-5810-8063
Tilley, Leann
Crabb, Brendan S.
Gilson, Paul R.
Journal name Cell Microbiology
Volume number 18
Issue number 11
Start page 1551
End page 1569
Total pages 19
Publisher Wiley-Blackwell
Place of publication Chichester, Eng.
Publication date 2016-11
ISSN 1462-5822
Summary The Plasmodium translocon for exported proteins (PTEX) has been established as the machinery responsible for the translocation of all classes of exported proteins beyond the parasitophorous vacuolar membrane of the intraerythrocytic malaria parasite. Protein export, particularly in the asexual blood stage, is crucial for parasite survival as exported proteins are involved in remodelling the host cell, an essential process for nutrient uptake, waste removal and immune evasion. Here, we have truncated the conserved C-terminus of one of the essential PTEX components, PTEX150, in Plasmodium falciparum in an attempt to create mutants of reduced functionality. Parasites tolerated C-terminal truncations of up to 125 amino acids with no reduction in growth, protein export or the establishment of new permeability pathways. Quantitative proteomic approaches however revealed a decrease in other PTEX subunits associating with PTEX150 in truncation mutants, suggesting a role for the C-terminus of PTEX150 in regulating PTEX stability. Our analyses also reveal three previously unreported PTEX-associated proteins, namely PV1, Pf113 and Hsp70-x (respective PlasmoDB numbers; PF3D7_1129100, PF3D7_1420700 and PF3D7_0831700) and demonstrate that core PTEX proteins exist in various distinct multimeric forms outside the major complex.
Language eng
DOI 10.1111/cmi.12596
Field of Research 060599 Microbiology not elsewhere classified
0605 Microbiology
1108 Medical Microbiology
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
Copyright notice ©2016, John Wiley & Sons
Persistent URL http://hdl.handle.net/10536/DRO/DU:30084872

Document type: Journal Article
Collection: Molecular and Medical Research
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