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Letters to Nature
Nature 379, 273 - 277 (18 January 1996); doi:10.1038/379273a0

Post-transcriptional transactivation of human retroviral envelope glycoprotein expression by herpes simplex virus Us11 protein

Jean-Jacques Diaz, Madeleine Due Dodon, Nathalie Schaerer-Uthurralt, Denis Simonin, Karine Kindbeiter, Louis Gazzolo & Jean-Jacques Madjar

Immuno-Virologie Moléculaire et Cellulaire, Université Claude Bernard Lyon-1/CNRS UMR30, Faculté de Médecine, rue Guillaume Paradin, 69372 Lyon CEDEX 08, France

HERPES simplex virus type 1 (HSV-1) Us11 protein, a true late gene product packaged within the virion, is delivered into cells after infection, exhibits a nucleocytoplasmic localization at early times, and later accumulates in the nucleoli1–5. This RNA-binding basic phosphoprotein, capable of oligomerization, is supposed to be involved in post-transcriptional regulation of gene expression after HSV-1 infection6,7. Expression of human T-cell leukaemia/ lymphoma virus type-I (HTLV-I) and of human immunodeficiency virus type 1 (HIV-1) is post-transcriptionally regulated by Rex and Rev, respectively8. These proteins are required for the cytoplasmic expression of unspliced gag-pol and singly spliced env transcripts9,10. Here we show that HSV-1 Us11 protein is able to bind Rex- and Rev-responsive elements and to transactivate envelope retroviral glycoprotein expression.

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