Journal article

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

K Matthews, M Kalanon, SA Chisholm, A Sturm, CD Goodman, MWA Dixon, PR Sanders, T Nebl, F Fraser, S Haase, GI Mcfadden, PR Gilson, BS Crabb, TF De Koning-Ward

Molecular Microbiology | WILEY | Published : 2013

Abstract

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 ..

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Grants

Awarded by Australian National Health and Medical Research Council


Funding Acknowledgements

We thank the Australian Red Cross for red blood cells. This work was supported by grants from the Australian National Health and Medical Research Council (533811) and Deakin University's Central Research Grants Scheme. M.K. acknowledges support from the Alfred Deakin Fellowship scheme. M.W.A.D. is an NHMRC Early Career Fellow. G.I.McF. is supported by a Program Grant from the NHMRC and a Discovery Grant from the Australian Research Council. T.F.d.K.-W. is supported by an NHMRC Career Development Fellowship.