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Updated: Oct 24, 2026

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
Published on: November 4, 2018
XPO1 coordinates human cytomegalovirus maturation by modulating genome encapsidation and secondary envelopment
Jin-Peng Wu1,2, Yue-Peng Zhou2,3, Meng-Jie Mei1,2
1State Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, 430071, China.
Abstract:
Human cytomegalovirus (HCMV) replication depends on tightly coordinated nuclear capsid assembly and cytoplasmic nucleocapsid maturation, yet host factors controlling these processes remain poorly defined. Here, we identify exportin 1 (XPO1) as a dual-phase regulator that coordinates HCMV maturation from nucleus to cytoplasm. XPO1 inhibition induces aberrant nuclear electron-dense speckles and accumulation of B-capsids. Mechanistically, nuclear retention of pp65 drives speckle formation but does not account for B-capsid accumulation. XPO1 recognizes a functional nuclear export signal (NES) within pUL77 and regulates its proper intranuclear localization. Inhibiting XPO1 or disrupting the NES induces intranuclear pUL77 aggregation and B-capsid accumulation. XPO1 is also required for viral assembly compartment formation and maintenance of late-stage autophagic flux, both of which are essential for secondary envelopment. Our findings highlight the key role of XPO1 in virion maturation and the therapeutic potential of repurposing FDA-approved XPO1 inhibitors as a host-directed antiviral strategy.
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