HSV

Herpes simplex virus type 1 (HSV-1) is a ubiquitous neurotropic pathogen that establishes lifelong latent infections in sensory neurons, primarily within trigeminal ganglia^[1][2]. Mechanistically, HSV-1 exploits host cellular factors, including heat-shock protein 90α (Hsp90α), to stabilize virion protein 16 (VP16) and facilitate transactivation of immediate-early α genes during lytic replication^[3][4]. Viral entry and spread are modulated by distinct classes of cellular glycans, with N-glycans essential for viral entry and propagation, O-glycans influencing glycoprotein gB and gD function, and glycosaminoglycans and glycolipids supporting viral attachment^[5]. In disease models, HSV-1 induces ocular pathologies such as herpetic stromal keratitis (HSK) and contributes to neurodegenerative features resembling Alzheimer’s disease, including tau hyperphosphorylation and amyloid-β accumulation^{[6][7][8][9][10]}. Compared with related isoforms, alternative splicing of host STING/TMEM173 produces truncated variants that selectively inhibit full-length STING, reducing IFN-β induction and allowing HSV-1 to evade innate immunity^[11]. Agonists and inhibitors targeting HSV-1 replication pathways demonstrate translational potential: oridonin suppresses viral replication via the NLRP3-inflammasome-IL-1β pathway, whereas SETD8 inhibition reduces immediate-early gene accessibility and lytic infection^[12][13]. These molecular insights provide frameworks for experimental applications, including antiviral drug screening, vaccine design, and mechanistic studies of viral-host interactions^[14][15][16].