Abstract
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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Diaz, JJ., Due Dodon, M., Schaerer-Uthurralt, N. et al. Post-transcriptional transactivation of human retroviral envelope glycoprotein expression by herpes simplex virus Us11 protein. Nature 379, 273–277 (1996). https://doi.org/10.1038/379273a0
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DOI: https://doi.org/10.1038/379273a0
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