The Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain

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Herpesviral capsid assembly is initiated in the host nucleus. Due to size constraints, newly formed nucleocapsids are unable to leave the nucleus through the nuclear pore complex. Instead herpesviruses apply an evolutionarily conserved mechanism for nuclear export of capsids called nuclear egress. This process is initiated by docking of capsids at the inner nuclear membrane, budding of enveloped capsids into the perinuclear space followed by de-envelopment and release of capsids to the cytoplasm where further maturation occurs. Two viral proteins conserved throughout the herpesvirus family, the membrane protein pUL34 and the phosphoprotein pUL31 form the nuclear egress complex that is critical for primary envelopment. We show here that pUL31 and pUL34 enter the nucleus independently of each other. pUL31 is targeted to the nucleoplasm where it binds to nucleocapsids via the conserved C-terminal domain, while its N-terminal domain is important for capsid translocation to the nuclear envelope and for a coordinated interaction with pUL34. Our data suggest a mechanism that is apparently conserved among all herpesviruses with pUL31 escorting nucleocapsids to the nuclear envelope in order to couple capsid maturation with primary envelopment.

Vyšlo v časopise: The Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain. PLoS Pathog 11(6): e32767. doi:10.1371/journal.ppat.1004957
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004957

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