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Human cytomegalovirus UL97 protein kinase is a serine/threonine viral kinase encoded by the UL97 gene of HCMV. It plays a pivotal role in viral replication by phosphorylating both viral and host cell proteins, manipulating processes such as cell cycle progression, virion morphogenesis, and egress of viral capsids from the nucleus[1][2][4][5][7]. The kinase is most notable in clinical medicine for its essential function in phosphorylating and activating the antiviral drug ganciclovir, and as the direct target of maribavir, a specific UL97 kinase inhibitor used in treatment of drug-resistant CMV infections[2][4][6]. Mutations in UL97 are a well-established mechanism of resistance to ganciclovir and maribavir, and sequencing this gene is used for resistance surveillance in clinical virology[6]. UL97 kinase is thus an established antiviral therapeutic target, particularly relevant in immunocompromised patient populations susceptible to CMV infection[2][4][8].
Phosphorylation of ganciclovir to its active antiviral form, enabling DNA polymerase inhibition; Inhibition by maribavir blocks kinase activity, disrupting viral replication and nuclear egress
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