The Plasmodium falciparum exported J domain proteins fine-tune human and malarial Hsp70s: Pathological exploitation of proteostasis machinery

This dataset represents the documentation and supporting information for the following published review article submitted to Frontiers in Molecular Biosciences: \"The Plasmodium falciparum exported J domain proteins fine-tune human and malarial Hsp70s: Pathological exploitation of proteostasis machinery\". This was an invited contribution to the following Section and Research Topic: Section: Protein Folding, Misfolding and Degradation; Research Topic: Guardians of Protein Homeostasis (Proteostasis) in Health, Disease and Aging. The intracellular malaria parasite, Plasmodium falciparum, has evolved the capacity to invade and transform mature human erythrocytes into vehicles of pathology. The parasite completely remodels the host cell by exporting numerous malaria proteins, including molecular chaperones and co-chaperones. The P. falciparum JDP (PfJDP) family is highly expanded with at least 49 members, and just under half predicted to be exported. The evidence suggests that there is an intricate network of PfJDP interactions with the exported malarial Hsp70 (PfHsp70-x) and human Hsp70, which appears to be important for the trafficking of key malarial virulence factors. This review critically evaluates the current understanding of the role of exported malarial JDPs in fine-tuning human and malarial Hsp70s, so as to re-set proteostasis for pathological purposes.