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P. falciparum heat shock response in a PfAP2-HS-defective population compared to its wild type control.

ABSTRACT: Periodic fever is the most characteristic clinical feature of human malaria. However, how parasites survive malarial febrile episodes, which often involve temperatures of >40ºC, is not known. Plasmodium falciparum cultures adapted to periodic heat shock were used to identify PfAP2-HS as a transcription factor that is essential for survival at febrile temperatures. Transcriptomic analysis was performed to compare the effect of heat shock in parasites presenting the wild type form of PfAP2-HS (10E) and parasites that have defects in this protein, either a premature stop codon mutation (10G) or the deletion of the entire pfap2-hs gene (10E_pfap2-hs). A timecourse analysis including samples taken before, during and after heat shock revealed that the initial phase of the PfAP2-HS-dependent response is largely restricted to hsp70-1 and hsp90.

ORGANISM(S): Plasmodium falciparum

PROVIDER: GSE149392 | GEO | 2021/05/17

REPOSITORIES: GEO

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Project description:Proctor2005 - Actions of chaperones and their role in ageing This model is described in the article: Modelling the actions of chaperones and their role in ageing. Proctor CJ, Soti C, Boys RJ, Gillespie CS, Shanley DP, Wilkinson DJ, Kirkwood TB. Mech. Ageing Dev. 2005 Jan; 126(1): 119-131 Abstract: Many molecular chaperones are also known as heat shock proteins because they are synthesised in increased amounts after brief exposure of cells to elevated temperatures. They have many cellular functions and are involved in the folding of nascent proteins, the re-folding of denatured proteins, the prevention of protein aggregation, and assisting the targeting of proteins for degradation by the proteasome and lysosomes. They also have a role in apoptosis and are involved in modulating signals for immune and inflammatory responses. Stress-induced transcription of heat shock proteins requires the activation of heat shock factor (HSF). Under normal conditions, HSF is bound to heat shock proteins resulting in feedback repression. During stress, cellular proteins undergo denaturation and sequester heat shock proteins bound to HSF, which is then able to become transcriptionally active. The induction of heat shock proteins is impaired with age and there is also a decline in chaperone function. Aberrant/damaged proteins accumulate with age and are implicated in several important age-related conditions (e.g. Alzheimer's disease, Parkinson's disease, and cataract). Therefore, the balance between damaged proteins and available free chaperones may be greatly disturbed during ageing. We have developed a mathematical model to describe the heat shock system. The aim of the model is two-fold: to explore the heat shock system and its implications in ageing; and to demonstrate how to build a model of a biological system using our simulation system (biology of ageing e-science integration and simulation (BASIS)). This model is hosted on BioModels Database and identified by: BIOMD0000000091. To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.

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P. falciparum heat shock response in a PfAP2-HS-defective population compared to its wild type control.

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