Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
, 13 (21), 5062-9

HSV-1 IE Protein Vmw110 Causes Redistribution of PML


HSV-1 IE Protein Vmw110 Causes Redistribution of PML

R D Everett et al. EMBO J.


Herpes simplex virus immediate-early protein Vmw110 is required for fully efficient viral gene expression and reactivation from latency. At early times of viral infection, Vmw110 localizes to discrete nuclear structures (known as ND10, PODs or Kr bodies) which contain several cellular proteins, including PML. Interestingly, the unregulated growth of promyelocytic leukaemia cells is correlated with disruption of the normal state of ND10. In this paper we show that: (i) Vmw110 affects the distribution of PML in the cell; (ii) Vmw110 proteins lacking a functional RING finger zinc-binding domain cause the production of striking abnormal cytoplasmic and nuclear structures, some of which contain PML and other ND10 antigens; (iii) a mutant form of Vmw110 which is confined to the cytoplasm appears to result in cytoplasmic PML in some cells; (iv) normal interaction with the nuclear structures requires the C-terminal portion of Vmw110; (v) the C-terminal portion of Vmw110, when linked to a heterologous protein, disrupts the normal distribution of PML. The results suggest that, in normal cells, the PML protein migrates between nucleus and cytoplasm. These observations present an unexpected link between processes involved in the control of cell growth and viral infection and latency.

Similar articles

See all similar articles

Cited by 195 PubMed Central articles

See all "Cited by" articles


    1. EMBO J. 1987 Jul;6(7):2069-76 - PubMed
    1. J Gen Virol. 1994 Jun;75 ( Pt 6):1223-33 - PubMed
    1. J Mol Biol. 1988 Jul 5;202(1):87-96 - PubMed
    1. J Gen Virol. 1989 May;70 ( Pt 5):1185-202 - PubMed
    1. J Virol. 1989 Aug;63(8):3513-5 - PubMed

Publication types

MeSH terms

LinkOut - more resources