Human cytomegalovirus tegument protein pp65 (pUL83) (pp65 (pUL83))

The Human cytomegalovirus tegument protein pp65 (pUL83) is the most abundant structural component of the HCMV virion tegument, comprising up to 15% of the particle mass, and serves as an optional scaffold that facilitates the incorporation of other tegument proteins such as pUL25, pUL69, and pUL97 into viral particles during morphogenesis.[1][2] Despite its abundance, pp65 is nonessential for virion formation or replication in fibroblasts, though its absence alters tegument composition, reduces particle size, impairs dense body formation, and hinders viral growth in cell types like monocyte-derived macrophages.[1][2][3] Functionally, pp65 modulates host innate immunity by inhibiting interferon-β production through binding and inactivating cGAS, blocking IRF-3 nuclear accumulation and phosphorylation, interacting with IFI16 to evade DNA sensing, and downregulating MHC class II expression and NK cell activity.[2][4][5] It is a major target for cellular T cell immune responses during HCMV infection, which causes severe disease in immunocompromised patients such as transplant recipients and congenitally infected infants.[2][3] While pp65 deletion mutants reveal its role in immune evasion and tegument assembly, no approved drugs directly target it, positioning it as a potential antiviral candidate in HCMV vaccine development focused on T cell induction.[3]

Other names

phosphoprotein 65ppUL83UL83pUL83