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Heat shock proteins and viral infection

Heat shock proteins (HSPs) are a kind of proteins which mostly found in bacterial, plant and animal cells, in which they are involved in the monitoring and regulation of cellular life activities. HSPs protect other proteins under environmental and cellular stress by regulating protein folding and su...

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Detalles Bibliográficos
Autores principales: Zhang, Xizhen, Yu, Wei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9389079/
https://www.ncbi.nlm.nih.gov/pubmed/35990630
http://dx.doi.org/10.3389/fimmu.2022.947789
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author Zhang, Xizhen
Yu, Wei
author_facet Zhang, Xizhen
Yu, Wei
author_sort Zhang, Xizhen
collection PubMed
description Heat shock proteins (HSPs) are a kind of proteins which mostly found in bacterial, plant and animal cells, in which they are involved in the monitoring and regulation of cellular life activities. HSPs protect other proteins under environmental and cellular stress by regulating protein folding and supporting the correctly folded structure of proteins as chaperones. During viral infection, some HSPs can have an antiviral effect by inhibiting viral proliferation through interaction and activating immune pathways to protect the host cell. However, although the biological function of HSPs is to maintain the homeostasis of cells, some HSPs will also be hijacked by viruses to help their invasion, replication, and maturation, thereby increasing the chances of viral survival in unfavorable conditions inside the host cell. In this review, we summarize the roles of the heat shock protein family in various stages of viral infection and the potential uses of these proteins in antiviral therapy.
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spelling pubmed-93890792022-08-20 Heat shock proteins and viral infection Zhang, Xizhen Yu, Wei Front Immunol Immunology Heat shock proteins (HSPs) are a kind of proteins which mostly found in bacterial, plant and animal cells, in which they are involved in the monitoring and regulation of cellular life activities. HSPs protect other proteins under environmental and cellular stress by regulating protein folding and supporting the correctly folded structure of proteins as chaperones. During viral infection, some HSPs can have an antiviral effect by inhibiting viral proliferation through interaction and activating immune pathways to protect the host cell. However, although the biological function of HSPs is to maintain the homeostasis of cells, some HSPs will also be hijacked by viruses to help their invasion, replication, and maturation, thereby increasing the chances of viral survival in unfavorable conditions inside the host cell. In this review, we summarize the roles of the heat shock protein family in various stages of viral infection and the potential uses of these proteins in antiviral therapy. Frontiers Media S.A. 2022-08-05 /pmc/articles/PMC9389079/ /pubmed/35990630 http://dx.doi.org/10.3389/fimmu.2022.947789 Text en Copyright © 2022 Zhang and Yu https://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) and the copyright owner(s) 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 Immunology
Zhang, Xizhen
Yu, Wei
Heat shock proteins and viral infection
title Heat shock proteins and viral infection
title_full Heat shock proteins and viral infection
title_fullStr Heat shock proteins and viral infection
title_full_unstemmed Heat shock proteins and viral infection
title_short Heat shock proteins and viral infection
title_sort heat shock proteins and viral infection
topic Immunology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9389079/
https://www.ncbi.nlm.nih.gov/pubmed/35990630
http://dx.doi.org/10.3389/fimmu.2022.947789
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