An Undefined Interaction between Polyamines and Heat Shock Proteins Leads to Cellular Protection in <i>Plasmodium falciparum</i> and Proliferating Cells in Various Organisms
Environmental stimuli can distress the internal reaction of cells and their normal function. To react promptly to sudden environmental changes, a cascade of heat shock proteins (Hsps) functions to protect and act as housekeepers inside the cells. In parallel to the heat shock response, the metabolic...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-02-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/28/4/1686 |
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| author | Xolani H. Makhoba Rino Ragno Annette Kaiser Enzo Agostinelli |
| author_facet | Xolani H. Makhoba Rino Ragno Annette Kaiser Enzo Agostinelli |
| author_sort | Xolani H. Makhoba |
| collection | DOAJ |
| description | Environmental stimuli can distress the internal reaction of cells and their normal function. To react promptly to sudden environmental changes, a cascade of heat shock proteins (Hsps) functions to protect and act as housekeepers inside the cells. In parallel to the heat shock response, the metabolic polyamine (PA) status changes. Here, we discuss possible ways of putative interactions between Hsps and polyamines in a wide lineage of eukaryotic model organisms with a particular focus on parasitic protozoa such as <i>Plasmodium falciparum</i> (<i>P. falciparum</i>). The supposed interaction between polyamines and Hsps may protect the parasite from the sudden change in temperature during transmission from the female <i>Anopheles</i> mosquito to a human host. Recent experiments performed with the spermidine mimetic inhibitor 15-deoxyspergualine in <i>Plasmodium</i> in vitro cultures show that the drug binds to the C-terminal EEVD motif of Hsp70. This leads to inhibition of protein biosynthesis caused by prevention of eIF5A2 phosphorylation and eukaryotic initiation factor 5A (eIF5A) modification. These observations provide further evidence that PAs are involved in the regulation of protein biosynthesis of Hsps to achieve a protective effect for the parasite during transmission. |
| first_indexed | 2024-03-11T08:22:24Z |
| format | Article |
| id | doaj.art-95db6e6d9fbd44ecb92984d9d0028641 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-11T08:22:24Z |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-95db6e6d9fbd44ecb92984d9d00286412023-11-16T22:21:52ZengMDPI AGMolecules1420-30492023-02-01284168610.3390/molecules28041686An Undefined Interaction between Polyamines and Heat Shock Proteins Leads to Cellular Protection in <i>Plasmodium falciparum</i> and Proliferating Cells in Various OrganismsXolani H. Makhoba0Rino Ragno1Annette Kaiser2Enzo Agostinelli3Department of Biochemistry, Microbiology, and Biotechnology, School of Molecular and Life Science, University of Limpopo, Turfloop Campus, Sovenga 0727, South AfricaRome Center for Molecular Design, Department of Drug Chemistry and Technology, Sapienza University, P. le A. Moro 5, 00185 Rome, ItalyMedical Research Centre, University of Duisburg-Essen, Hufeland Strasse 55, 45147 Essen, GermanyDepartment of Sensory Organs, Sapienza University of Rome, Policlinico Umberto I, Viale del Policlinico 155, 00161 Rome, ItalyEnvironmental stimuli can distress the internal reaction of cells and their normal function. To react promptly to sudden environmental changes, a cascade of heat shock proteins (Hsps) functions to protect and act as housekeepers inside the cells. In parallel to the heat shock response, the metabolic polyamine (PA) status changes. Here, we discuss possible ways of putative interactions between Hsps and polyamines in a wide lineage of eukaryotic model organisms with a particular focus on parasitic protozoa such as <i>Plasmodium falciparum</i> (<i>P. falciparum</i>). The supposed interaction between polyamines and Hsps may protect the parasite from the sudden change in temperature during transmission from the female <i>Anopheles</i> mosquito to a human host. Recent experiments performed with the spermidine mimetic inhibitor 15-deoxyspergualine in <i>Plasmodium</i> in vitro cultures show that the drug binds to the C-terminal EEVD motif of Hsp70. This leads to inhibition of protein biosynthesis caused by prevention of eIF5A2 phosphorylation and eukaryotic initiation factor 5A (eIF5A) modification. These observations provide further evidence that PAs are involved in the regulation of protein biosynthesis of Hsps to achieve a protective effect for the parasite during transmission.https://www.mdpi.com/1420-3049/28/4/1686polyaminesheat shock proteins<i>Plasmodium falciparum</i>plants and drug discoverycancer |
| spellingShingle | Xolani H. Makhoba Rino Ragno Annette Kaiser Enzo Agostinelli An Undefined Interaction between Polyamines and Heat Shock Proteins Leads to Cellular Protection in <i>Plasmodium falciparum</i> and Proliferating Cells in Various Organisms Molecules polyamines heat shock proteins <i>Plasmodium falciparum</i> plants and drug discovery cancer |
| title | An Undefined Interaction between Polyamines and Heat Shock Proteins Leads to Cellular Protection in <i>Plasmodium falciparum</i> and Proliferating Cells in Various Organisms |
| title_full | An Undefined Interaction between Polyamines and Heat Shock Proteins Leads to Cellular Protection in <i>Plasmodium falciparum</i> and Proliferating Cells in Various Organisms |
| title_fullStr | An Undefined Interaction between Polyamines and Heat Shock Proteins Leads to Cellular Protection in <i>Plasmodium falciparum</i> and Proliferating Cells in Various Organisms |
| title_full_unstemmed | An Undefined Interaction between Polyamines and Heat Shock Proteins Leads to Cellular Protection in <i>Plasmodium falciparum</i> and Proliferating Cells in Various Organisms |
| title_short | An Undefined Interaction between Polyamines and Heat Shock Proteins Leads to Cellular Protection in <i>Plasmodium falciparum</i> and Proliferating Cells in Various Organisms |
| title_sort | undefined interaction between polyamines and heat shock proteins leads to cellular protection in i plasmodium falciparum i and proliferating cells in various organisms |
| topic | polyamines heat shock proteins <i>Plasmodium falciparum</i> plants and drug discovery cancer |
| url | https://www.mdpi.com/1420-3049/28/4/1686 |
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