Herpesviruses encode homologues of cellular basic leucine zipper (bZIP) transcription factors that are key regulators of both viral and host gene expression. Among these, MEQ from Marek’s disease virus, Zta from Epstein-Barr virus, and K-bZIP from Kaposi’s sarcoma-associated herpesvirus are critical virulence factors that facilitate viral replication, immune evasion, and oncogenesis by controlling nuclear transcriptional programs. These viral bZIPs traffic to the host cell nucleus, a process mediated by the host importin α/β transport machinery, which recognize specific nuclear localization signals (NLS) within proteins. This study investigates the nuclear import mechanisms of these bZIPs by characterizing their interactions with the host importin α/β complex. Electrophoretic mobility shift assays (EMSA) demonstrated that predicted NLS sequences from MEQ, Ztaand K-bZIP bind to members of each of the three importin-α subfamilies, and directly to importin-β proteins. Fluorescence polarization (FP) assays quantified binding affinities, revealing that MEQ exhibits high affinity for importin-α isoforms (Kd range: 5.55-11.93 nM) and Importin β isoforms (Kd range: 1.54-25.5 nM). Zta showed lower affinity for importin α isoforms (Kd range: 53.4-1431 nM) and selective binding to importin β2 (Kd = 107.0 nM). K-bZIP displayed moderate affinity for importin α isoforms (Kd range: 45.64-254.0 nM) and selective binding to importin β2 (Kd = 230.9 nM). X-ray crystallography of the MEQ-importin α2 complex (2.3 Å resolution) revealed that MEQ residues 29-36 engage both minor and major binding sites of importin-α2. These findings suggest that each viral bZIP engages the importin complex via distinct NLS sequences, potentially modulating nuclear import efficiency and specificity. Understanding these mechanisms advances our knowledge of herpesvirus pathogenesis and identifies potential antiviral targets for disrupting critical protein-protein interactions required for nuclear localization and transcriptional regulation.