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Experimental analysis shows that parasite-derived J-domains stimulate ATPase activity in HSP70, suggesting chaperone exploitation in host cells.
The malaria parasite P. falciparum exports a large number of proteins to the human host cell, including members of the J‐domain protein (JDP) family. In other systems, JDPs stimulate the ATPase activity of HSP70 and direct client protein interactions. Three exported Pf JDP are highly homologous yet appear to have divergent roles. We examined the ability of isolated J‐domains from these proteins to stimulate the ATPase activity of Pf HSP70‐X and human Hs HSP70 and Hs HSC70. In vitro assays demonstrate that all domains stimulate the ATPase activity of each HSP70 tested. While overall stimulation was broadly comparable, differences were observed between individual Pf JDP–HSP70 pairings. Our findings support a model in which the parasite systematically exports JDPs to exploit the host's chaperone power.
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Barth et al. (2026) studied this question.
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