Plasmodium falciparum HSP40 protein eCiJp traffics to the erythrocyte cytoskeleton and interacts with the human HSP70 chaperone HSPA1

Welka Sahu; Tapaswini Bai; Pritam Kumar Panda; Archita Mazumder; Aleena Das; Deepak Kumar Ojha; Suresh K Verma; Selvakumar Elangovan; K Sony Reddy

doi:10.1002/1873-3468.14255

Plasmodium falciparum HSP40 protein eCiJp traffics to the erythrocyte cytoskeleton and interacts with the human HSP70 chaperone HSPA1

FEBS Lett. 2022 Jan;596(1):95-111. doi: 10.1002/1873-3468.14255. Epub 2021 Dec 18.

Authors

Welka Sahu¹, Tapaswini Bai¹, Pritam Kumar Panda², Archita Mazumder¹, Aleena Das^{1

3}, Deepak Kumar Ojha¹, Suresh K Verma¹, Selvakumar Elangovan¹, K Sony Reddy¹

Affiliations

¹ School of Biotechnology, Kalinga Institute of Industrial Technology, Deemed to be University, Bhubaneswar, India.
² Condensed Matter Theory Group, Materials Theory Division, Department of Physics and Astronomy, Uppsala University, Sweden.
³ Technology Business Incubator, Kalinga Institute of Industrial Technology, Deemed to be University, Bhubaneswar, India.

PMID: 34890056
DOI: 10.1002/1873-3468.14255

Abstract

Renovation of host erythrocytes is vital for pathogenesis by Plasmodium falciparum. These changes are mediated by parasite proteins that translocate beyond the parasitophorous vacuolar membrane in an unfolded state, suggesting protein folding by chaperones is imperative for the functionality of exported proteins. We report a type IV P. falciparum heat-shock protein 40, PF11_0034, that localizes to the cytoplasmic side of J-dots and interacts with the erythrocyte cytoskeleton, and therefore named eCiJp (erythrocyte cytoskeleton-interacting J protein). Recombinant eCiJp binds to the human heat-shock protein 70 HsHSPA1 and promotes its ATPase activity. In addition, eCiJp could suppress protein aggregation. Our data suggest that eCiJp recruits HsHSPA1 to the host erythrocyte cytoskeleton, where it may become involved in remodeling of the erythrocyte cytoskeleton and/or folding of exported parasite proteins.

Keywords: HSP40; HSPA1; blood stage malaria; erythrocyte cytoskeleton interaction; heat-shock proteins; host-pathogen interaction.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

HSP40 Heat-Shock Proteins*

Substances

HSP40 Heat-Shock Proteins