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Abstract
Poxviruses are large DNA viruses that include the causal agent of human smallpox and
vaccinia virus. Poxviruses replicate in cytoplasmic foci known as DNA factories. Here
we show that a virus-encoded transcription factor, viral mRNA, cellular RNA-binding
protein heterodimer G3BP/Caprin-1 (p137), translation initiation factors eIF4E and
eIF4G, and ribosomal proteins are concentrated in the same subdomains of cytoplasmic
DNA factories. Furthermore, a cell coinfected with two recombinant vaccinia viruses
expressing a virus core protein fused to cyan or yellow fluorescent protein displayed
separate cyan and yellow factories, indicating that each factory formed from a single
genome and was the site of transcription and translation as well as DNA replication.
Hijacking of the host translation apparatus within the factory likely enhances the
efficiency of virus replication and contributes to the suppression of host protein
synthesis, thereby facilitating poxvirus subjugation of the cell.