Protein export in malaria parasites: do multiple export motifs add up to multiple export pathways?

Spielmann, Tobias; Gilberger, Tim‐Wolf

doi:10.1016/j.pt.2009.10.001

Cited by 106 publications

(117 citation statements)

References 54 publications

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“…Our findings apply for different types of proteins, the major group of exported proteins containing a PEXEL motif 2 represented by RIFIN A 29 as well as for PEXEL negative exported proteins such as SBP1 and REX2 (ref. 53). Protein export uncoupled from cleft genesis is more versatile: it allows for an appropriately timed and tuned export cas cade to deliver proteins to all Maurer's clefts.…”

Section: Discussionmentioning

confidence: 99%

Development and host cell modifications of Plasmodium falciparum blood stages in four dimensions

et al. 2011

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Blood stages of Plasmodium falciparum cause the pathology of malaria; however, the progression of the parasite through this complex part of the life cycle has never been visualized. In this study, we use four-dimensional imaging to show for the first time the development of individual parasites in erythrocytes and the concomitant host cell modifications. our data visualize an unexpectedly dynamic parasite, provide a reference for this life cycle stage and challenge the model that protein export in P. falciparum is linked to the biogenesis of host cell modifications termed maurer's clefts. our results provide a novel view of the blood-stage development, maurer's cleft development and protein export in malaria parasites, and open the door to study dynamic processes, drug effects and the phenotype of mutants.

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Section: Discussionmentioning

confidence: 99%

Development and host cell modifications of Plasmodium falciparum blood stages in four dimensions

et al. 2011

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“…This "exportome" provides the basis to study exported proteins and their involvement in the pathology of remodeled infected erythrocytes much more specifically. Besides the defined PEXEL exportome, there are additional exported proteins that lack a known or discernible export element, referred to as PEXEL-negative proteins (PNEPs) (13,14). Although the definitive number of proteins exported into the erythrocyte is unknown, it is without doubt that they play important roles in pathology through the significant changes that they induce in infected erythrocytes and that they are major contributors to disease.…”

Section: Protein Exportmentioning

confidence: 99%

Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling

Warncke

Vakonakis

Beck

2016

Microbiol Mol Biol Rev

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SUMMARYDuring the asexual cycle,Plasmodium falciparumextensively remodels the human erythrocyte to make it a suitable host cell. A large number of exported proteins facilitate this remodeling process, which causes erythrocytes to become more rigid, cytoadherent, and permeable for nutrients and metabolic products. Among the exported proteins, a family of 89 proteins, called thePlasmodiumhelical interspersed subtelomeric (PHIST) protein family, has been identified. While also found in otherPlasmodiumspecies, the PHIST family is greatly expanded inP. falciparum. Although a decade has passed since their first description, to date, most PHIST proteins remain uncharacterized and are of unknown function and localization within the host cell, and there are few data on their interactions with other host or parasite proteins. However, over the past few years, PHIST proteins have been mentioned in the literature at an increasing rate owing to their presence at various localizations within the infected erythrocyte. Expression of PHIST proteins has been implicated in molecular and cellular processes such as the surface display of PfEMP1, gametocytogenesis, changes in cell rigidity, and also cerebral and pregnancy-associated malaria. Thus, we conclude that PHIST proteins are central to host cell remodeling, but despite their obvious importance in pathology, PHIST proteins seem to be understudied. Here we review current knowledge, shed light on the definition of PHIST proteins, and discuss these proteins with respect to their localization and probable function. We take into consideration interaction studies, microarray analyses, or data from blood samples from naturally infected patients to combine all available information on this protein family.

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“…[14][15][16] A number of exported proteins do not contain a PEXEL/VTS motif and are thus called PEXEL-negative exported proteins (PNEPs); their transport pathways are unknown. 5,17 Various proteins play a role in trafficking PfEMP1 to the P falciparum-infected RBC membrane and its assembly into knob structures (reviewed in Maier et al protein 1 (MAHRP1), 21 or ring-exported protein 1 (REX1), 22 PfEMP1 cannot be displayed on the RBC membrane. Additionally, a largescale gene-knockout screen in P falciparum identified other proteins required for trafficking and function of PfEMP1.…”

Section: Introductionmentioning

confidence: 99%

Export of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeleton

Rug

Cyrklaff

Mikkonen

et al. 2014

Blood

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Protein export in malaria parasites: do multiple export motifs add up to multiple export pathways?

Cited by 106 publications

References 54 publications

Development and host cell modifications of Plasmodium falciparum blood stages in four dimensions

Development and host cell modifications of Plasmodium falciparum blood stages in four dimensions

Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling

Export of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeleton

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