Protein export in Plasmodium parasites: from the endoplasmic reticulum to the vacuolar export machine
- PMID: 20170656
- DOI: 10.1016/j.ijpara.2010.02.002
Protein export in Plasmodium parasites: from the endoplasmic reticulum to the vacuolar export machine
Abstract
It is somewhat paradoxical that the malaria parasite's survival strategy involves spending almost all of its blood-stage existence residing behind a two-membrane barrier in a host red blood cell, yet giving considerable attention to exporting parasite-encoded proteins back across these membranes. These exported proteins are thought to play diverse roles and are crucial in pathogenic processes, such as re-modelling of the erythrocyte cytoskeleton and mediating the export of a major virulence protein known as Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1), and in metabolic processes such as nutrient uptake and solute exchange. Despite these varied roles most exported proteins have at least one common link; they share a trafficking pathway that begins with entry into the endoplasmic reticulum and concludes with passage across the vacuole membrane via a proteinaceous translocon known as the Plasmodium translocon of exported proteins (PTEX). In this commentary we review recent advances in our understanding of this export pathway and suggest several models by which different aspects of the process may be interconnected.
2010 Australian Society for Parasitology Inc. Published by Elsevier Ltd. All rights reserved.
Similar articles
-
New insights into protein export in malaria parasites.Cell Microbiol. 2010 May 1;12(5):580-7. doi: 10.1111/j.1462-5822.2010.01455.x. Epub 2010 Feb 19. Cell Microbiol. 2010. PMID: 20180801 Review.
-
Two putative protein export regulators promote Plasmodium blood stage development in vivo.Mol Biochem Parasitol. 2013 Sep;191(1):44-52. doi: 10.1016/j.molbiopara.2013.09.003. Epub 2013 Sep 25. Mol Biochem Parasitol. 2013. PMID: 24076174
-
Recent insights into the export of PEXEL/HTS-motif containing proteins in Plasmodium parasites.Curr Opin Microbiol. 2012 Dec;15(6):699-704. doi: 10.1016/j.mib.2012.09.008. Epub 2012 Oct 22. Curr Opin Microbiol. 2012. PMID: 23092921 Review.
-
PTEX is an essential nexus for protein export in malaria parasites.Nature. 2014 Jul 31;511(7511):587-91. doi: 10.1038/nature13555. Epub 2014 Jul 16. Nature. 2014. PMID: 25043043
-
Targeting malaria virulence and remodeling proteins to the host erythrocyte.Science. 2004 Dec 10;306(5703):1930-3. doi: 10.1126/science.1102452. Science. 2004. PMID: 15591202
Cited by
-
The mature N-termini of Plasmodium effector proteins confer specificity of export.mBio. 2023 Oct 31;14(5):e0121523. doi: 10.1128/mbio.01215-23. Epub 2023 Aug 30. mBio. 2023. PMID: 37646514 Free PMC article.
-
Ancient class of translocated oomycete effectors targets the host nucleus.Proc Natl Acad Sci U S A. 2010 Oct 5;107(40):17421-6. doi: 10.1073/pnas.1008491107. Epub 2010 Sep 16. Proc Natl Acad Sci U S A. 2010. PMID: 20847293 Free PMC article.
-
The exported chaperone Hsp70-x supports virulence functions for Plasmodium falciparum blood stage parasites.PLoS One. 2017 Jul 21;12(7):e0181656. doi: 10.1371/journal.pone.0181656. eCollection 2017. PLoS One. 2017. PMID: 28732045 Free PMC article.
-
Structure of the catalytic domain of Plasmodium falciparum ARF GTPase-activating protein (ARFGAP).Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt 11):1339-44. doi: 10.1107/S1744309111032507. Epub 2011 Oct 25. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011. PMID: 22102228 Free PMC article.
-
An image-based drug susceptibility assay targeting the placental sequestration of Plasmodium falciparum-infected erythrocytes.PLoS One. 2012;7(8):e41765. doi: 10.1371/journal.pone.0041765. Epub 2012 Aug 29. PLoS One. 2012. PMID: 22952585 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials