- Title
- Plasmodium falciparum Hop (PfHop) interacts with the Hsp70 chaperone in a nucleotide-dependent fashion and exhibits ligand selectivity
- Creator
- Zininga, Tawanda
- Creator
- Makumire, Stanley
- Creator
- Gitau, Grace W
- Creator
- Njunge, James M
- Creator
- Pooe, Ofentse J
- Creator
- Klimek, Hanna
- Creator
- Scheurr, Robina
- Creator
- Raifer, Hartmann
- Creator
- Prinsloo, Earl
- Creator
- Przyborski, Jude M
- Creator
- Hoppe, Heinrich C
- Creator
- Shonhai, Addmore
- Subject
- To be catalogued
- Date Issued
- 2015
- Date
- 2015
- Type
- text
- Type
- article
- Identifier
- http://hdl.handle.net/10962/431752
- Identifier
- vital:72801
- Identifier
- xlink:href=" https://doi.org/10.1371/journal.pone.0135326"
- Description
- Heat shock proteins (Hsps) play an important role in the development and pathogenicity of malaria parasites. One of the most prominent functions of Hsps is to facilitate the folding of other proteins. Hsps are thought to play a crucial role when malaria parasites invade their host cells and during their subsequent development in hepatocytes and red blood cells. It is thought that Hsps maintain proteostasis under the unfavourable conditions that malaria parasites encounter in the host environment. Although heat shock protein 70 (Hsp70) is capable of independent folding of some proteins, its functional cooperation with heat shock protein 90 (Hsp90) facilitates folding of some proteins such as kinases and steroid hormone receptors into their fully functional forms. The cooperation of Hsp70 and Hsp90 occurs through an adaptor protein called Hsp70-Hsp90 organising protein (Hop). We previously characterised the Hop protein from Plasmodium falciparum (PfHop). We observed that the protein co-localised with the cytosol-localised chaperones, PfHsp70-1 and PfHsp90 at the blood stages of the malaria parasite. In the current study, we demonstrated that PfHop is a stress-inducible protein. We further explored the direct interaction between PfHop and PfHsp70-1 using far Western and surface plasmon resonance (SPR) analyses.
- Format
- computer
- Format
- online resource
- Format
- application/pdf
- Format
- 1 online resource (15 pages)
- Format
- Publisher
- PLOSOne
- Language
- English
- Relation
- PLoS One
- Relation
- Zininga, T., Makumire, S., Gitau, G.W., Njunge, J.M., Pooe, O.J., Klimek, H., Scheurr, R., Raifer, H., Prinsloo, E., Przyborski, J.M. and Hoppe, H., 2015. Plasmodium falciparum Hop (PfHop) interacts with the Hsp70 chaperone in a nucleotide-dependent fashion and exhibits ligand selectivity. PLoS One, 10(8), p.e0135326
- Relation
- PLoS One volume 10 number 8 p.e0135326 2015 1932-6203
- Rights
- Publisher
- Rights
- Use of this resource is governed by the terms and conditions of the PLOSOne Terms of Use Statement (https://www.plos.org/terms-of-use)
- Rights
- Open Access
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Collections
Prinsloo, Earl (Dr)
RU DST/NRF SARChI for Biotechnology Innovation and Engagement
Hoppe, Heinrich C (Prof)
RU Department of Biochemistry, Microbiology and Bioinformatics
SDG 03. Good Health and Well-Being
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