Herpes simplex virus type 2 tegument protein UL25 (UL25)

Herpes simplex virus type 2 (HSV-2) tegument protein UL25 is a critical structural component of the viral capsid, primarily located at the vertices of the icosahedral shell [9, 31]. It plays a multifaceted role in the viral life cycle, including stabilizing the capsid to withstand the high internal pressure of the packaged double-stranded DNA genome and facilitating the nuclear egress of mature capsids [4, 35, 38]. Additionally, UL25 is involved in the early stages of infection, where it assists in the uncoating and release of the viral genome into the host nucleus [18, 31]. Due to its essential and highly conserved nature across the Herpesviridae family, UL25 is a prominent target for the development of novel therapeutic vaccines and antiviral agents [4, 24]. Research has shown that UL25 is a major target for CD8+ T-cell responses in infected individuals, making it a key candidate for subunit vaccines aimed at reducing viral shedding and recurrence [24, 34]. While no small-molecule inhibitors are currently approved for clinical use, experimental studies have explored UL25-derived peptides and other strategies to disrupt its function in capsid assembly and egress [23, 33].

Other names

Protein UL25pUL25Minor capsid protein UL25DNA packaging protein UL25Capsid-associated tegument protein UL25

Inhibition of capsid stabilization, blocking of DNA packaging, or prevention of nuclear egress