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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 chapero...

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Autores principales: Przyborski, Jude M., Diehl, Mathias, Blatch, Gregory L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4481151/
https://www.ncbi.nlm.nih.gov/pubmed/26167469
http://dx.doi.org/10.3389/fmolb.2015.00034
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author Przyborski, Jude M.
Diehl, Mathias
Blatch, Gregory L.
author_facet Przyborski, Jude M.
Diehl, Mathias
Blatch, Gregory L.
author_sort Przyborski, Jude M.
collection PubMed
description 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.
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spelling pubmed-44811512015-07-10 Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle Przyborski, Jude M. Diehl, Mathias Blatch, Gregory L. Front Mol Biosci Molecular Biosciences 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. Frontiers Media S.A. 2015-06-26 /pmc/articles/PMC4481151/ /pubmed/26167469 http://dx.doi.org/10.3389/fmolb.2015.00034 Text en Copyright © 2015 Przyborski, Diehl and Blatch. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Przyborski, Jude M.
Diehl, Mathias
Blatch, Gregory L.
Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle
title Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle
title_full Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle
title_fullStr Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle
title_full_unstemmed Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle
title_short Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle
title_sort plasmodial hsp70s are functionally adapted to the malaria parasite life cycle
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4481151/
https://www.ncbi.nlm.nih.gov/pubmed/26167469
http://dx.doi.org/10.3389/fmolb.2015.00034
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