Mathias Diehl
University of Marburg
VacuoleMembrane proteinAdaptationTransloconImmunologyProtein foldingHeat shock proteinMalariaCompartment (chemistry)Plasmodium falciparumPlasmodium (life cycle)Host cell cytosolLife styleGeneticsHsp70Parasite hostingBiologyCell biology
2Publications
2H-index
30Citations
Publications 3
Newest
#1Mathias DiehlH-Index: 2
#2L. Roling (University of Giessen)H-Index: 1
Last. Julia Hahn (University of Giessen)H-Index: 1
view all 13 authors...
The pathology associated with malaria infection is largely due to the ability of infected human RBCs to adhere to a number of receptors on endothelial cells within tissues and organs. This phenomenon is driven by the export of parasite-encoded proteins to the host cell, the exact function of many of which is still unknown. Here we inactivate the function of one of these exported proteins, PFA66, a member of the J-domain protein family. Although parasites lacking this protein were still able to g...
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#1Anke Tribensky (University of Marburg)H-Index: 3
#2Andreas W. Graf (University of Marburg)H-Index: 1
Last. Jude M. Przyborski (University of Marburg)H-Index: 28
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Having entered the mature human erythrocyte, the malaria parasite survives and propagates within a parasitophorous vacuole, a membrane-bound compartment separating the parasite from the host cell cytosol. The bounding membrane of this vacuole, referred to as the parasitophorous vacuolar membrane (PVM), contains parasite-encoded proteins, but how these membrane proteins are trafficked to the PVM remains unknown. Here, we have studied the trafficking of PfExp1 to the PVM. We find that trafficking ...
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#1Jude M. PrzyborskiH-Index: 28
#2Mathias DiehlH-Index: 2
Last. Gregory L. Blatch (VU: Victoria University, Australia)H-Index: 39
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The human malaria parasite, Plasmodium falciparum, encodes a minimal complement of six heat shock protein 70s (PfHSP70s), some of which are highly expressed and are thought to play an important role in the survival and pathology of the parasite. In addition to canonical features of molecular chaperones, these HSP70s possess properties that reflect functional adaptation to a parasitic life style, including resistance to thermal insult during fever periods and host-parasite interactions. The paras...
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