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Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies

In recent studies we and others have identified the cellular proteins PML, hDaxx, and Sp100, which form a subnuclear structure known as nuclear domain 10 (ND10) or PML nuclear bodies (PML-NBs), as host restriction factors that counteract herpesviral infections by inhibiting viral replication at diff...

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Detalles Bibliográficos
Autores principales: Tavalai, Nina, Stamminger, Thomas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3185544/
https://www.ncbi.nlm.nih.gov/pubmed/21994592
http://dx.doi.org/10.3390/v1031240
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author Tavalai, Nina
Stamminger, Thomas
author_facet Tavalai, Nina
Stamminger, Thomas
author_sort Tavalai, Nina
collection PubMed
description In recent studies we and others have identified the cellular proteins PML, hDaxx, and Sp100, which form a subnuclear structure known as nuclear domain 10 (ND10) or PML nuclear bodies (PML-NBs), as host restriction factors that counteract herpesviral infections by inhibiting viral replication at different stages. The antiviral function of ND10, however, is antagonized by viral regulatory proteins (e.g., ICP0 of herpes simplex virus; IE1 of human cytomegalovirus) which induce either a modification or disruption of ND10. This review will summarize the current knowledge on how viral replication is inhibited by ND10 proteins. Furthermore, herpesviral strategies to defeat this host defense mechanism are discussed.
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spelling pubmed-31855442011-10-12 Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies Tavalai, Nina Stamminger, Thomas Viruses Review In recent studies we and others have identified the cellular proteins PML, hDaxx, and Sp100, which form a subnuclear structure known as nuclear domain 10 (ND10) or PML nuclear bodies (PML-NBs), as host restriction factors that counteract herpesviral infections by inhibiting viral replication at different stages. The antiviral function of ND10, however, is antagonized by viral regulatory proteins (e.g., ICP0 of herpes simplex virus; IE1 of human cytomegalovirus) which induce either a modification or disruption of ND10. This review will summarize the current knowledge on how viral replication is inhibited by ND10 proteins. Furthermore, herpesviral strategies to defeat this host defense mechanism are discussed. Molecular Diversity Preservation International (MDPI) 2009-12-15 /pmc/articles/PMC3185544/ /pubmed/21994592 http://dx.doi.org/10.3390/v1031240 Text en © 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Tavalai, Nina
Stamminger, Thomas
Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies
title Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies
title_full Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies
title_fullStr Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies
title_full_unstemmed Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies
title_short Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies
title_sort interplay between herpesvirus infection and host defense by pml nuclear bodies
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3185544/
https://www.ncbi.nlm.nih.gov/pubmed/21994592
http://dx.doi.org/10.3390/v1031240
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