Key result
Co-expressing viral helicase-primase components UL5, UL8, and UL52 enables efficient nuclear localization.
The UL8 protein appears to facilitate the nuclear uptake of the herpes simplex virus type 1 helicase-primase complex.
May guide HSV-1 antiviral strategies targeting nuclear import; leaves open validation in human cells.
We constructed recombinant viruses based on the herpes simplex virus type 1 mutant tsK which individually were able to express the products of four viral DNA replication genes (UL5, UL8, UL9 and UL52) in the absence of any of the other proteins required for viral DNA synthesis. These viruses were used in immunofluorescence experiments to investigate the cellular localization of the four replication proteins expressed. The results demonstrated that all three components of the viral helicase-primase complex (UL5, UL8 and UL52 proteins) must be co-expressed to allow their efficient localization to the nucleus. Since the UL5 and UL52 proteins together form a complex which is enzymatically indistinguishable from a complex formed from all three proteins, a possible role of the UL8 protein may be in facilitating nuclear uptake. The UL9 protein (origin-binding protein) efficiently entered the cell nucleus when expressed alone. Both UL9 protein and the tripartite helicase-primase complex exhibited patterns of fluorescence which resembled the 'pre-replicative sites' described previously.
No takes yet. Share an insight, caveat, or question.
Calder et al. (1992) studied Herpes simplex virus type 1. Recombinant viruses expressing UL5, UL8, UL9, and UL52 was evaluated on Cellular localization of viral replication proteins. Co-expression of all three components of the viral helicase-primase complex (UL5, UL8, and UL52) is required for their efficient localization to the nucleus.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: