Major capsid protein UL19 (VP5)

Major capsid protein UL19, also known as VP5, is the primary structural component of the icosahedral capsid in Herpes Simplex Virus (HSV-1 and HSV-2) [1, 2]. It forms the hexons and pentons that constitute the viral shell, protecting the double-stranded DNA genome [2, 3]. UL19 is essential for the assembly of the procapsid and its subsequent maturation into the infectious C-capsid [2, 21]. Beyond its structural role, it interacts with host factors like dynactin for nuclear transport and is involved in the ejection of viral DNA into the host nucleus [16, 21]. Due to its conservation and critical function in the viral life cycle, UL19 is a significant target for the development of novel antivirals, including small molecule assembly inhibitors and RNA interference therapies [8, 17]. These approaches are particularly valuable for treating acyclovir-resistant strains, as they target a different stage of the viral life cycle than traditional polymerase inhibitors [17, 23]. Experimental therapies such as meganucleases and siRNAs have demonstrated the potential to significantly reduce viral load by targeting the UL19 gene or its protein product [17, 22]. However, challenges remain in delivering these agents to the nucleus and overcoming the potential for viral resistance through mutations in the capsid structure [13, 16].

Other names

VP5UL19Major capsid protein VP5HHV1gp028ICP5Capsid protein VP5

Inhibition of viral capsid assembly [21], disruption of DNA packaging [17], and silencing of viral gene expression [17].