Publications & Reports

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

Matthews K, Kalanon M, Chisholm SA, Sturm A, Goodman CD, Dixon MW, Sanders PR, Nebl T, Fraser F, Haase S, McFadden GI, Gilson PR, Crabb BS, de Koning-Ward TF
School of Medicine, Deakin University, Waurn Ponds, Victoria, 3216, Australia.


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 P. 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, whilst not essential for parasite survival, TRX2 may help to optimise PTEX activity. Importantly, the generation of TRX2 knockout parasites that display altered phenotypes provides a much-needed tool to dissect PTEX function.



  • Journal: Molecular Microbiology
  • Published: 22/07/2013
  • Volume: 89
  • Issue: 6
  • Pagination: 1167-1186


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