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Varicella-zoster virus proteins comprise the diverse set of functional proteins encoded by the genome of **Varicella-zoster virus (VZV)**, a human-restricted **alphaherpesvirus** that is the causative agent of chickenpox (varicella) and shingles (herpes zoster)[4][6][2]. The viral proteome includes more than 70 proteins, functionally classified as **structural proteins** (capsid, envelope glycoproteins, tegument components), **enzymes** (such as DNA polymerase, kinases, nucleases, and the DNA helicase-primase complex), and **regulatory factors** like the major immediate-early protein 62 (IE62)[4][6][2]. Key viral glycoproteins (notably **gB, gH, and gL** among others) mediate fusion with host cells, enabling viral entry and spread[3][4][7][9]. Capsid proteins assemble into complex icosahedral structures critical for viral genome packaging and virion stability[1][4]. Immediate-early regulatory proteins direct transcription of viral genes and manipulate the host cell environment to support infection and immune evasion[4][2]. Some VZV proteins, such as the DNA polymerase, are the **primary molecular targets of antiviral drugs** (e.g., acyclovir, valacyclovir), while others (for example, components of the fusion complex or capsid) are being investigated as novel therapeutic targets[3][1][9]. Detection of VZV DNA or specific viral proteins is the molecular basis for diagnostic tests and may be used as **biomarkers** for infection or vaccine response. **Note:** "Varicella-zoster virus proteins" is a broad, collective category and does not refer to a single molecular target; structured information is best constructed for individual proteins (e.g., "Varicella-zoster virus glycoprotein B"). This entry is flagged as *is_incorrect* because it is not specific to a single molecular target as typically defined in drug discovery or pharmacology[1][2][3][4][9].
Inhibition of viral DNA polymerase, Inhibition of viral replication, Potential capsid assembly or fusion inhibition
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