The Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-x

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The Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-x

Plasmodium falciparum, the human pathogen responsible for the most dangerous malaria infection, survives and develops in mature erythrocytes through the export of proteins needed for remodelling of the host cell. Molecular chaperones of the heat shock protein (Hsp) family are prominent members of the exportome, including a number of Hsp40s and a Hsp70. PFA0660w, a type II Hsp40, has been shown ...

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Proteomic analysis of exported chaperone/co-chaperone complexes of P. falciparum reveals an array of complex protein-protein interactions

Malaria parasites modify their human host cell, the mature erythrocyte. This modification is mediated by a large number of parasite proteins that are exported to the host cell, and is also the underlying cause for the pathology caused by malaria infection. Amongst these proteins are many Hsp40 co-chaperones, and a single Hsp70. These proteins have been implicated in several processes in the hos...

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Plasmodium falciparum Hsp70-x: a heat shock protein at the host-parasite interface.

Plasmodium falciparum 70 kDa heat shock proteins (PfHsp70s) are expressed at all stages of the pathogenic erythrocytic phase of the malaria parasite life cycle. There are six PfHsp70s, all of which have orthologues in other plasmodial species, except for PfHsp70-x which is unique to P. falciparum. This research highlights a number of original results obtained by a detailed bioinformatics analys...

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ژورنال

عنوان ژورنال: PLOS ONE

سال: 2016

ISSN: 1932-6203

DOI: 10.1371/journal.pone.0148517