Overexpression, purification and characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) protein.

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dc.citation.doi10.1371/journal.pone.0129445en_ZA
dc.citation.issue6en_ZA
dc.contributor.authorZininga, T.
dc.contributor.authorHoppe, H.C.
dc.contributor.authorPrinsloo.E.
dc.contributor.authorDirr, H.W.
dc.contributor.authorShonhai, A.
dc.contributor.authorAchilonu, I.
dc.date.accessioned2016-09-16T10:10:47Z
dc.date.available2016-09-16T10:10:47Z
dc.date.issued2015-06-17
dc.description.abstractSix Hsp70-like genes are represented on the genome of Plasmodium falciparum. Of these two occur i0n the cytosol: P. falciparum Hsp70-z (PfHsp70-z) and PfHsp70-1. PfHsp70-1 is a well characterised canonical Hsp70 that facilitates protein quality control and is crucial for the development of malaria parasites. There is very little known about PfHsp70-z. However, PfHsp70-z is known to be essential and is implicated in suppressing aggregation of asparagine-rich proteins of P. falciparum. In addition, its expression at the clinical stage of malaria correlates with disease prognosis. Based on structural evidence PfHsp70-z belongs to the Hsp110 family of proteins. Since Hsp110 proteins have been described as nucleotide exchange factors (NEFs) of their canonical Hsp70 counterparts, it has been speculated that PfHsp70-z may serve as a NEF of PfHsp70-1. In the current study, P. falciparum cells cultured in vitro were subjected to heat stress, triggering the enhanced expression of PfHsp70-z. Biochemical assays conducted using recombinant PfHsp70-z protein demonstrated that the protein is heat stable and possesses ATPase activity. Furthermore, we observed that PfHsp70-z is capable of self-association. The structural-functional features of PfHsp70-z provide further evidence for its role as a chaperone and possible nucleotide exchange factor of PfHsp70-1.en_ZA
dc.description.librarianNCS2016en_ZA
dc.description.sponsorshipThis project was through a grant (L1/402/ 14-1) provided to AS by the Deutsche Forchungsgemeinshaft (DFG) under the theme, “German–African Cooperation Projects in Infectology”. The authors are grateful to the Department of Science and Technology/National Research Foundation (NRF) of South Africa for providing an equipment grant (grant UID, 75464) to AS and (grant UID, 78558) to EP. HWD was awarded a research grant (64788) by the NRF (South Africa). AS is a recipient of a Georg Foster researchen_ZA
dc.identifier.citationZininga, T. et al. 2015. Overexpression, purification and characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) protein. PLOS ONE 10(6):e0129445en_ZA
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/10539/21038
dc.journal.titlePLOS ONEen_ZA
dc.journal.volume10en_ZA
dc.language.isoenen_ZA
dc.publisherPublic Library of Science.en_ZA
dc.rights© 2015 Zininga et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en_ZA
dc.subjectadenosine triphosphatase;en_ZA
dc.subjectchaperone;en_ZA
dc.subjectheat shock protein 70;en_ZA
dc.subjectcontrolled study;en_ZA
dc.subjectcross reaction;en_ZA
dc.subjectenzyme activity;en_ZA
dc.subjectgene;en_ZA
dc.subjectgene overexpression;en_ZA
dc.subjectheat stress;en_ZA
dc.subjectheat stress;en_ZA
dc.subjectHsp70 gene;en_ZA
dc.subjectmalaria; nonhuman;en_ZA
dc.subjectPlasmodium falciparum;en_ZA
dc.subjectprotein aggregation;en_ZA
dc.subjectprotein expression;en_ZA
dc.subjectprotein purification;en_ZA
dc.subjectprotein secondary structure;en_ZA
dc.subjectstructure analysis;en_ZA
dc.subjecttemperature;en_ZA
dc.subjectupregulationen_ZA
dc.subjectPlasmodium falciparum;en_ZA
dc.titleOverexpression, purification and characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) protein.en_ZA
dc.typeArticleen_ZA
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