M. Meredith et al., SEPARATION OF SEQUENCE REQUIREMENTS FOR HSV-1 VMW11O MULTIMERIZATION AND INTERACTION WITH A 135-KDA CELLULAR PROTEIN, Virology, 209(1), 1995, pp. 174-187
Herpes simplex virus type 1 immediate-early polypeptide Vmw110 (ICP0)
is a general transactivator of gene expression in transfection assays
and is required for the fully efficient onset of viral lyric replicati
on. It has also been implicated in the process of viral reactivation f
rom latency. Its mechanism of action is unknown, but any involvement i
n latency requires interactions between viral and host factors. We hav
e previously shown that Vmw110 binds to a 135-kDa cellular protein. In
this paper we define a short region towards the C-terminal end of Vmw
110 that is required for the 135-kDa protein interaction in virus-infe
cted cells and in vitro. We also confirm that the C-terminal region of
Vmw110 contains residues that are responsible for the multimerisation
of the protein; these sequences are at least partially distinct from
those involved in 135-kDa binding. Both multimerisation and 135-kDa pr
otein interaction are required for full viral infectivity, and elimina
tion of these functions affects the normal interactions between Vmw110
and cellular nuclear structures that contain the PML protein. (C) 199
5 Academic Press, Inc.