A pUL25 dimer interfaces the pseudorabies virus capsid and tegument

Yun Tao Liu, Jiansen Jiang, Kevin Patrick Bohannon, Xinghong Dai, G. W. Gant Luxton, Wong Hoi Hui, Guo Qiang Bi, Gregory Allan Smith, Z. Hong Zhou*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


Inside the virions of α-herpesviruses, tegument protein pUL25 anchors the tegument to capsid vertices through direct interactions with tegument proteins pUL17 and pUL36. In addition to promoting virion assembly, both pUL25 and pUL36 are critical for intracellular microtubule-dependent capsid transport. Despite these essential roles during infection, the stoichiometry and precise organization of pUL25 and pUL36 on the capsid surface remain controversial due to the insufficient resolution of existing reconstructions from cryo-electron microscopy (cryoEM). Here, we report a threedimensional (3D) icosahedral reconstruction of pseudorabies virus (PRV), a varicellovirus of the α-herpesvirinae subfamily, obtained by electron-counting cryoEM at 4.9 Å resolution. Our reconstruction resolves a dimer of pUL25 forming a capsidassociated tegument complex with pUL36 and pUL17 through a coiled coil helix bundle, thus correcting previous misinterpretations. A comparison between reconstructions of PRV and the γ-herpesvirus Kaposi’s sarcoma-associated herpesvirus (KSHV) reinforces their similar architectures and establishes important subfamily differences in the capsid-tegument interface.

Original languageEnglish (US)
Article number000903
Pages (from-to)2837-2849
Number of pages13
JournalJournal of General Virology
Issue number11
StatePublished - Nov 2017


  • CryoEM
  • PUL17
  • PUL25 dimer
  • PUL36 (VP1/2)
  • Pseudorabies virus
  • Tegument proteins

ASJC Scopus subject areas

  • Virology


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