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

Daniyan, Michael O; Boshoff, Aileen; Prinsloo, Earl; Pesce, Eva-Rachele; Blatch, Gregory L

Title: The Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-x
Creator: Daniyan, Michael O
Creator: Boshoff, Aileen
Creator: Prinsloo, Earl
Creator: Pesce, Eva-Rachele
Creator: Blatch, Gregory L
Date Issued: 2016
Date: 2016
Type: text
Type: article
Identifier: http://hdl.handle.net/10962/66098
Identifier: vital:28901
Identifier: https://doi.org/10.1371/journal.pone.0148517
Description: publisher version
Description: 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 to be exported and possibly form a complex with PfHsp70-x in the infected erythrocyte cytosol. However, the chaperone properties of PFA0660w and its interaction with human and parasite Hsp70s are yet to be investigated. Recombinant PFA0660w was found to exist as a monomer in solution, and was able to significantly stimulate the ATPase activity of PfHsp70-x but not that of a second plasmodial Hsp70 (PfHsp70-1) or a human Hsp70 (HSPA1A), indicating a potential specific functional partnership with PfHsp70-x. Protein binding studies in the presence and absence of ATP suggested that the interaction of PFA0660w with PfHsp70-x most likely represented a co-chaperone/chaperone interaction. Also, PFA0660w alone produced a concentration-dependent suppression of rhodanese aggregation, demonstrating its chaperone properties. Overall, we have provided the first biochemical evidence for the possible role of PFA0660w as a chaperone and as co-chaperone of PfHsp70-x. We propose that these chaperones boost the chaperone power of the infected erythrocyte, enabling successful protein trafficking and folding, and thereby making a fundamental contribution to the pathology of malaria.
Description: This work was supported by grants from the National Research Foundation (NRF) and Medical Research Council (MRC) of South Africa. The ProteOn XPR36 IAS was purchased from a National Nanotechnology Equipment Programme grant from the Department of Science and Technology and the NRF of South Africa. Michael O. Daniyan was a recipient of the Education Trust Fund (ETF) Academic Staff Training and Development (AST and D) scholarship of Obafemi Awolowo University, Ile-Ife, Nigeria and a Rhodes University Council research bursary
Format: 13 pages
Format: pdf
Language: English
Relation: PLOS ONE
Relation: Daniyan, M.O., Boshoff, A., Prinsloo, E., Pesce, E-R., Blatch, G.L. (2016) The Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-x. PLoS ONE 11(2). doi:10.1371/journal.pone.0148517
Relation: PLOS ONE volume 11 number 2 1 13 February 2016 1932-6203
Rights: Copyright held by the authors
Rights: Use of this resource is governed by the terms and conditions of the PLOS ONE Open Access Statement (http://journals.plos.org/plosone/s/journal-information#loc-open-access)

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RU Department of Biochemistry, Microbiology and Biotechnology

Prinsloo, Earl (Dr)

SDG 03. Good Health and Well-Being

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