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Journal of Virology, January 2000, p. 99-109, Vol. 74, No. 1
0022-538X/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Analysis of HCF, the Cellular Cofactor of VP16,
in Herpes Simplex Virus-Infected Cells
Sylvie
LaBoissière and
Peter
O'Hare*
Marie Curie Research Institute, Oxted, Surrey
RH8 OTL, United Kingdom
Received 13 July 1999/Accepted 17 September 1999
Herpes simplex virus (HSV) immediate-early (IE) gene expression is
initiated via the recruitment of the structural protein VP16 onto
specific sites upstream of each IE gene promoter in a multicomponent
complex (TRF.C) that also includes the cellular proteins Oct-1 and HCF.
In vitro results have shown that HCF binds directly to VP16 and
stabilizes TRF.C. Results from transfection assays have also indicated
that HCF is involved in the nuclear import of VP16. However, there have
been no reports on the role or the fate of HCF during HSV type 1 (HSV-1) infection. Here we show that the intracellular distribution of
HCF is dramatically altered during HSV-1 infection and that the protein
interacts with and colocalizes with VP16. Moreover, viral protein
synthesis and replication were significantly reduced after infection of a BHK-21-derived temperature-sensitive cell line (tsBN67)
which contains a mutant HCF unable to associate with VP16 at the
nonpermissive temperature. Intracellular distribution of HCF and of
newly synthesized VP16 in tsBN67-infected cells was similar
to that observed in Vero cells, suggesting that late in infection the
trafficking of both proteins was not dependent on their association. We
constructed a stable cell line (tsBN67r) in which the
temperature-sensitive phenotype was rescued by using an epitope-tagged
wild-type HCF. In HSV-1-infected tsBN67r cells at the
nonpermissive temperature, direct binding of HCF to VP16 was observed,
but virus protein synthesis and replication were not restored to levels
observed at the permissive temperature or in wild-type BHK cells.
Together these results indicate that the factors involved in
compartmentalization of VP16 alter during infection and that late in
infection, VP16 and HCF may have additional roles reflected in their
colocalization in replication compartments.
*
Corresponding author. Mailing address: Marie Curie
Research Institute, The Chart, Oxted, Surrey RH8 OTL, United Kingdom.
Phone: 1883-722306. Fax: 1883-714375. E-mail:
P.O'Hare{at}mcri.ac.uk.
Journal of Virology, January 2000, p. 99-109, Vol. 74, No. 1
0022-538X/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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