Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies

Nina Tavalai; Thomas Stamminger

doi:10.3390/v1031240

Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies

Viruses. 2009 Dec;1(3):1240-64. doi: 10.3390/v1031240. Epub 2009 Dec 15.

Authors

Nina Tavalai¹, Thomas Stamminger

Affiliation

¹ Institute for Clinical and Molecular Virology, University of Erlangen-Nuremberg, Schlossgarten 4, 91054 Erlangen, Germany; E-Mail: nina.tavalai@viro.med.uni-erlangen.de.

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: PML; PML nuclear bodies; Sp100; antiviral defense; hDaxx; herpesvirus; interferon; intrinsic immunity; nuclear domain 10.