Abstract
Viruses have evolved diverse strategies to exploit the compartmentalized architecture of eukaryotic cells, particularly by targeting the nuclear envelope (NE) and its associated nuclear pore complexes (NPCs). The NE, composed of a double-membrane lipid bilayer, NPCs, and the nuclear lamina, establishes a physical barrier that protects genetic material in the nucleus from harmful cytosolic agents while enabling the spatial segregation of transcription and translation. This compartmentalization allows eukaryotic cells to tightly regulate gene expression, a process that requires the bidirectional shuttling of macromolecules such as transcription factors and messenger ribonucleoprotein particles across the NE. The NPC is the sole gateway to the nucleus and is essential for protein biogenesis, metabolic homeostasis, and cell survival. In this review, we examine how viruses remodel NPC architecture, hijack nucleocytoplasmic transport, and disable host innate immune responses to enhance viral replication.