Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle

The human malaria parasite, Plasmodium falciparum, encodes a minimal complement of six heat shock protein 70s (PfHSP70s), some of which are highly expressed and are thought to play an important role in the survival and pathology of the parasite. In addition to canonical features of molecular chaperones, these HSP70s possess properties that reflect functional adaptation to a parasitic life style, including resistance to thermal insult during fever periods and host–parasite interactions. The parasite even exports an HSP70 to the host cell where it is likely to be involved in host cell modification. This review focuses on the features of the PfHSP70s, particularly with respect to their adaptation to the malaria parasite life cycle.

• Publication year

  2015

• Venue

  Frontiers in Molecular Biosciences

• Publication date

  2015-06-26

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.3389/fmolb.2015.00034PMID 26167469PMCID 4481151
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• [Plasmodium falciparum].

  2022cited by this paper
• PFB0595w is a Plasmodium falciparum J protein that co-localizes with PfHsp70-1 and can stimulate its in vitro ATP hydrolysis activity.

  2015cited by this paper
• Overexpression, Purification and Characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) Protein

  2015cited by this paper
• Are Heat Shock Proteins Druggable Candidates

  2014cited by this paper
• PTEX is an essential nexus for protein export in malaria parasites

  2014cited by this paper
• Selective modulation of plasmodial Hsp70s by small molecules with antimalarial activity

  2014cited by this paper
• Plasmodial Hsp40 and Hsp70 chaperones: current and future perspectives

  2014cited by this paper
• Faculty Opinions recommendation of PTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytes.

  2014cited by this paper
• HSP101/PTEX mediates export of diverse malaria effector proteins into the host erythrocyte

  2014cited by this paper
• Plasmodium falciparum Hsp70-x: a heat shock protein at the host–parasite interface

  2013cited by this paper
• Identification of New PNEPs Indicates a Substantial Non-PEXEL Exportome and Underpins Common Features in Plasmodium falciparum Protein Export

  2013cited by this paper
• Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers

  2012cited by this paper
• Hsp70s and J proteins of Plasmodium parasites infecting rodents and primates: structure, function, clinical relevance, and drug targets.

  2012cited by this paper
• Wherever I may roam: protein and membrane trafficking in P. falciparum-infected red blood cells.

  2012influential reference
• Plasmodium falciparum‐encoded exported hsp70/hsp40 chaperone/co‐chaperone complexes within the host erythrocyte

  2012influential reference
• Redox-Dependent Protein Quality Control in the Endoplasmic Reticulum: Folding to Degradation

  2012cited by this paper
• Uncovering common principles in protein export of malaria parasites.

  2012cited by this paper
• Targeting Conserved Pathways as a Strategy for Novel Drug Development: Disabling the Cellular Stress Response

  2012cited by this paper
• Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock

  2011cited by this paper
• The apicomplexan plastid and its evolution

  2011influential reference
• Expression of a Malarial Hsp70 Improves Defects in Chaperone-Dependent Activities in ssa1 Mutant Yeast

  2011cited by this paper
• Intracellular protozoan parasites of humans: the role of molecular chaperones in development and pathogenesis.

  2011cited by this paper
• World malaria report 2011

  2011influential reference
• Screening for small molecule modulators of Hsp70 chaperone activity using protein aggregation suppression assays: inhibition of the plasmodial chaperone PfHsp70-1

  2011influential reference
• Characterisation of the Plasmodium falciparum Hsp70–Hsp90 organising protein (PfHop)

  2011cited by this paper
• Protein export in malaria parasites: do multiple export motifs add up to multiple export pathways?

  2010cited by this paper
• Plasmodial heat shock proteins: targets for chemotherapy.

  2010cited by this paper
• Parasite‐encoded Hsp40 proteins define novel mobile structures in the cytosol of the P. falciparum‐infected erythrocyte

  2010influential reference
• Malaria heat shock proteins: drug targets that chaperone other drug targets.

  2010cited by this paper
• Hsp70-1 from Plasmodium falciparum: protein stability, domain analysis and chaperone activity.

  2009influential reference
• A novel twist to protein secretion in eukaryotes.

  2009cited by this paper
• An Unusual ERAD-Like Complex Is Targeted to the Apicoplast of Plasmodium falciparum

  2009influential reference
• Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum

  2009cited by this paper
• An aspartyl protease directs malaria effector proteins to the host cell

  2009cited by this paper
• The philosophy of scientific experimentation: a review

  2009cited by this paper
• A glimpse into the clinical proteome of human malaria parasites Plasmodium falciparum and Plasmodium vivax

  2009cited by this paper
• A novel protein export machine in malaria parasites

  2009cited by this paper
• Plasmepsin V licenses Plasmodium proteins for export into the host erythrocyte

  2009cited by this paper
• Select pyrimidinones inhibit the propagation of the malarial parasite, Plasmodium falciparum.

  2009cited by this paper
• Exported Proteins Required for Virulence and Rigidity of Plasmodium falciparum-Infected Human Erythrocytes

  2008cited by this paper
• The Plasmodium falciparum heat shock protein 40, Pfj4, associates with heat shock protein 70 and shows similar heat induction and localisation patterns.

  2008influential reference
• N-terminal processing of proteins exported by malaria parasites.

  2008cited by this paper
• Structure-function study of a Plasmodium falciparum Hsp70 using three dimensional modelling and in vitro analyses.

  2008cited by this paper
• Transport of nuclear-encoded proteins into secondarily evolved plastids

  2007cited by this paper
• Unraveling the components of protein translocation pathway in human malaria parasite Plasmodium falciparum.

  2007cited by this paper
• The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum

  2007cited by this paper
• The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host.

  2007influential reference
• Lineage-specific expansion of proteins exported to erythrocytes in malaria parasites

  2006influential reference
• 15-Deoxyspergualin modulates Plasmodium falciparum heat shock protein function.

  2006influential reference
• Plasmodium falciparum heat shock protein 70 is able to suppress the thermosensitivity of an Escherichia coli DnaK mutant strain

  2005cited by this paper
• Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70.

  2004cited by this paper
• A Host-Targeting Signal in Virulence Proteins Reveals a Secretome in Malarial Infection

  2004cited by this paper
• Targeting Malaria Virulence and Remodeling Proteins to the Host Erythrocyte

  2004cited by this paper
• CIS AND TRANS FACTORS INVOLVED IN APICOPLAST TARGETING IN TOXOPLASMA GONDII

  2003cited by this paper
• The Signal Sequence of Exported Protein-1 Directs the Green Fluorescent Protein to the Parasitophorous Vacuole of Transfected Malaria Parasites*

  2003cited by this paper
• Dissecting Apicoplast Targeting in the Malaria Parasite Plasmodium falciparum

  2003cited by this paper
• Effect of heat‐shock on Plasmodium falciparum viability, growth and expression of the heat‐shock protein ‘PFHSP70‐I’ gene

  1992cited by this paper
• Nucleotide sequence of a Plasmodium falciparum stress protein with similarity to mammalian 78-kDa glucose-regulated protein.

  1992cited by this paper
• Induction and localization of Plasmodium falciparum stress proteins related to the heat shock protein 70 family.

  1991influential reference
• Plasmodium falciparum gene encoding a protein similar to the 78-kDa rat glucose-regulated stress protein.

  1988cited by this paper

• The impact of Iso-mukaadial acetate on Plasmodium falciparum transcriptional gene regulation

  2025cites this paper
• Plasmodium falciparum heat shock proteins as antimalarial drug targets: An update

  2024cites this paper
• Nanotechnology based drug delivery systems for malaria.

  2024cites this paper
• Proteostasis is a key driver of the pathogenesis in Apicomplexa.

  2024cites this paper
• Controlling drug resistance by targeting Plasmodium falciparum heat shock protein 70-1, a chaperone at the centre of protein quality control mechanism: a review

  2023cites this paper
• The artemisinin-induced dormant stages of Plasmodium falciparum exhibit hallmarks of cellular quiescence/senescence and drug resilience

  2023cites this paper
• Insertion of GGMP repeat residues of Plasmodium falciparum Hsp70-1 in the lid of DnaK adversely impacts client recognition.

  2023cites this paper
• An Undefined Interaction between Polyamines and Heat Shock Proteins Leads to Cellular Protection in Plasmodium falciparum and Proliferating Cells in Various Organisms

  2023cites this paper
• Exported J domain proteins of the human malaria parasite

  2022cites this paper
• Plasmodium falciparum Molecular Chaperones: Guardians of the Malaria Parasite Proteome and Renovators of the Host Proteome

  2022cites this paper
• A non-traditional crystal-based compound screening method targeting the ATP binding site of Plasmodium falciparum GRP78 for identification of novel nucleoside analogues

  2022cites this paper
• HSP70 and their co-chaperones in the human malaria parasite P. falciparum and their potential as drug targets

  2022cites this paper
• The Role of Hsp70s in the Development and Pathogenicity of Plasmodium falciparum.

  2021cites this paper
• General Structural and Functional Features of Molecular Chaperones.

  2021cites this paper
• Iso-mukaadial acetate and ursolic acid acetate inhibit the chaperone activity of Plasmodium falciparum heat shock protein 70-1

  2021cites this paper
• The Role of Malaria Parasite Heat Shock Proteins in Protein Trafficking and Remodelling of Red Blood Cells.

  2021cites this paper
• Heat Shock Proteins of Malaria: Highlights and Future Prospects.

  2021cites this paper
• Role of the J Domain Protein Family in the Survival and Pathogenesis of Plasmodium falciparum.

  2021cites this paper
• Introductory Chapter: The Importance of Heat Shock Proteins in Survival and Pathogenesis of the Malaria Parasite Plasmodium falciparum.

  2021cites this paper
• Heat Shock Proteins as Targets for Novel Antimalarial Drug Discovery.

  2021cites this paper
• Lipid transport proteins in malaria, from plasmodium parasites to their hosts.

  2021cites this paper
• Exported plasmodial J domain protein, PFE0055c, and PfHsp70-x form a specific co-chaperone-chaperone partnership

  2020cites this paper
• Comparative Characterization of Plasmodium falciparum Hsp70-1 Relative to E. coli DnaK Reveals the Functional Specificity of the Parasite Chaperone

  2020cites this paper
• Comparative characterisation of Plasmodium falciparum Hsp70-1 relative to E. coli DnaK reveals functional specificity of the parasite chaperone

  2020influential citation
• Detection of Protein Aggregation in Live Plasmodium Parasites

  2020cites this paper
• Characterization of Hsp70 gene family provides insight into its functions related to microsporidian proliferation.

  2020cites this paper
• Crossing the Vacuolar Rubicon: Structural Insights into Effector Protein Trafficking in Apicomplexan Parasites

  2020cites this paper
• Structural-functional diversity of malaria parasite's PfHSP70-1 and PfHSP40 chaperone pair gives an edge over human orthologs in chaperone-assisted protein folding.

  2020cites this paper
• Chaperoning of asparagine repeat-containing proteins in Plasmodium falciparum

  2020cites this paper
• Plasmodium yoelii Uses a TLR3-Dependent Pathway to Achieve Mammalian Host Parasitism

  2020cites this paper
• PV1 Protein from Plasmodium falciparum Exhibits Chaperone-Like Functions and Cooperates with Hsp100s

  2020cites this paper
• Comparative structure-function features of Hsp70s of Plasmodium falciparum and human origins

  2019cites this paper
• Partners in Mischief: Functional Networks of Heat Shock Proteins of Plasmodium falciparum and Their Influence on Parasite Virulence

  2019cites this paper
• Establishing Computational Approaches Towards Identifying Malarial Allosteric Modulators: A Case Study of Plasmodium falciparum Hsp70s

  2019cites this paper
• Comparative analysis of a chimeric Hsp70 of E. coli and Plasmodium falciparum origin relative to its wild type forms

  2019cites this paper
• Investigation of the role of the GGMP motif of Plasmodium falciparum Hsp70-1 on the chaperone function of the protein and its interaction with a co-chaperone, PfHop

  2019influential citation
• The 70 KDA Heat Shock Protein Hsp70 as Part of a Protein Disaggregase System

  2018cites this paper
• Molecular Chaperones Involved in Protein Recovery from Aggregates are Present in Protozoa Causative of Malaria and Leishmaniasis

  2018cites this paper
• Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis

  2018cites this paper
• Expression of monocyte heat shock protein 70 (HSP70) during malaria fever in the presence of antimalarial, anti-inflammatory drugs and β-haematin.

  2017cites this paper
• Antiplasmodial activity of Warburgia salutaris (Bertol. F.) Chiov. (Cannelaceae).

  2017cites this paper
• Introduction: Second Edition

  2017cites this paper
• The Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-x

  2016cites this paper
• Characterization of heat shock protein 70-z (PfHsp70-z) from plasmodium falciparium

  2015influential citation