Viruses 2009, 1(3), 1240-1264; doi:10.3390/v1031240
Review

Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies

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Received: 18 November 2009; in revised form: 10 December 2009 / Accepted: 14 December 2009 / Published: 15 December 2009
(This article belongs to the Special Issue Antiviral Responses to Herpes Viruses)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract: 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.
Keywords: herpesvirus; nuclear domain 10; PML nuclear bodies; PML; Sp100; hDaxx; antiviral defense; intrinsic immunity; interferon
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MDPI and ACS Style

Tavalai, N.; Stamminger, T. Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies. Viruses 2009, 1, 1240-1264.

AMA Style

Tavalai N, Stamminger T. Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies. Viruses. 2009; 1(3):1240-1264.

Chicago/Turabian Style

Tavalai, Nina; Stamminger, Thomas. 2009. "Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies." Viruses 1, no. 3: 1240-1264.


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