Disease relevance of UL17

• The distribution of UL17 and UL25 on B capsids was examined using immunogold labeling [1].
• The UL17 protein of herpes simplex virus type 1 is essential for packaging the viral genome into the procapsid, a spherical assembly intermediate, and is present in the mature virus particle [2].
• To analyze UL17 of pseudorabies virus (PrV) the complete 597-amino-acid protein was expressed in Escherichia coli and used for rabbit immunization [3].
• Homologs of the UL17 gene of the alphaherpesvirus herpes simplex virus 1 (HSV-1) are conserved in all three subfamilies of herpesviruses [3].

High impact information on UL17

• Herpes simplex virus type 1 DNA-packaging protein UL17 is required for efficient binding of UL25 to capsids [1].
• The results suggest that UL17 is a minor capsid protein which is incorporated into the procapsid during assembly of the particle [2].
• Functional characterization of PrV-DeltaUL17F, a deletion mutant lacking codons 23 to 444, demonstrated that cleavage of viral DNA into unit-length genomes was inhibited in the absence of UL17 [3].
• Cells infected with the UL17 mutant virus also displayed UL6-specific fluorescence in a diffuse pattern at the nuclear periphery in regions not containing ICP35 and ICP5 [4].

Biological context of UL17

• The properties of the UL17 and UL25 proteins are consistent with the idea that the two proteins are important in stabilizing capsid-DNA structures rather than having a direct role in DNA packaging [1].
• We conclude that the UL17 gene is required for correct targeting of capsids and major and minor capsid proteins to the DNA replication compartment of HEp-2 cells and deduce that this targeting reflects one functional role of UL17 in viral DNA cleavage and packaging [4].

Other interactions of UL17

• In the absence of UL17, the levels of UL25 in the mutant capsids were much lower than those in wt B capsids [1].

References