Openly accessible

The Plasmodium translocon of exported proteins (PTEX) component thioredoxin-2 is important for maintaining normal blood-stage growth

Matthews, Kathryn, Kalanon, Ming, Chisholm, Scott A, Sturm, Angelika, Goodman, Christopher D, Dixon, Matthew W A, Sanders, Paul R, Nebl, Thomas, Fraser, Fiona, Haase, Silvia, McFadden, Geoffrey I, Gilson, Paul R, Crabb, Brendan S and de Koning-Ward, Tania F 2013, The Plasmodium translocon of exported proteins (PTEX) component thioredoxin-2 is important for maintaining normal blood-stage growth, Molecular microbiology, vol. 89, no. 6, pp. 1167-1186, doi: 10.1111/mmi.12334.

Attached Files
Name Description MIMEType Size Downloads
matthews-plasmodiumtrans-post-2013.pdf Author's post print application/pdf 529.57KB 228

Title The Plasmodium translocon of exported proteins (PTEX) component thioredoxin-2 is important for maintaining normal blood-stage growth
Author(s) Matthews, Kathryn
Kalanon, Ming
Chisholm, Scott A
Sturm, Angelika
Goodman, Christopher D
Dixon, Matthew W A
Sanders, Paul R
Nebl, Thomas
Fraser, Fiona
Haase, Silvia
McFadden, Geoffrey I
Gilson, Paul R
Crabb, Brendan S
de Koning-Ward, Tania FORCID iD for de Koning-Ward, Tania F orcid.org/0000-0001-5810-8063
Journal name Molecular microbiology
Volume number 89
Issue number 6
Start page 1167
End page 1186
Total pages 20
Publisher Wiley-Blackwell Publishing
Place of publication Chichester, England
Publication date 2013-08
ISSN 0950-382X
1365-2958
Keyword(s) plasmodium parasites
cerebral malaria model
Summary Plasmodium parasites remodel their vertebrate host cells by translocating hundreds of proteins across an encasing membrane into the host cell cytosol via a putative export machinery termed PTEX. Previously PTEX150, HSP101 and EXP2 have been shown to be bona fide members of PTEX.

Here we validate that PTEX88 and TRX2 are also genuine members of PTEX and provide evidence that expression of PTEX components are also expressed in early gametocytes, mosquito and liver stages, consistent with observations that protein export is not restricted to asexual stages. Although amenable to genetic tagging, HSP101, PTEX150, EXP2 and PTEX88 could not be genetically deleted in Plasmodium berghei, in keeping with the obligatory role this complex is postulated to have in maintaining normal blood-stage growth.

In contrast, the putative thioredoxin-like protein TRX2 could be deleted, with knockout parasites displaying reduced grow-rates, both in vivo and in vitro, and reduced capacity to cause severe disease in a cerebral malaria model. Thus, while not essential for parasite survival, TRX2 may help to optimize PTEX activity. Importantly, the generation of TRX2 knockout parasites that display altered phenotypes provides a much-needed tool to dissect PTEX function.
Language eng
DOI 10.1111/mmi.12334
Field of Research 110801 Medical Bacteriology
Socio Economic Objective 920109 Infectious Diseases
HERDC Research category C1 Refereed article in a scholarly journal
Grant ID NHMRC 533811
NHMRC 1006091
Copyright notice ©2013, Wiley-Blackwell Publishing
Free to Read? Yes
Persistent URL http://hdl.handle.net/10536/DRO/DU:30055461

Document type: Journal Article
Collections: 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 37 times in TR Web of Science
Scopus Citation Count Cited 37 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 375 Abstract Views, 238 File Downloads  -  Detailed Statistics
Created: Tue, 27 Aug 2013, 15:11:24 EST by Jane Moschetti

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.