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Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies
Institute for Clinical and Molecular Virology, University of Erlangen-Nuremberg, Schlossgarten 4, 91054 Erlangen, Germany
* Author to whom correspondence should be addressed.
Received: 18 November 2009; in revised form: 10 December 2009 / Accepted: 14 December 2009 / Published: 15 December 2009
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.
Tavalai N, Stamminger T. Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies. Viruses. 2009; 1(3):1240-1264.
Tavalai, Nina; Stamminger, Thomas. 2009. "Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies." Viruses 1, no. 3: 1240-1264.