By the same authors

From the same journal

Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex

Research output: Contribution to journalArticlepeer-review


  • Benjamin G Butt
  • Danielle J Owen
  • Cy M Jeffries
  • Lyudmila Ivanova
  • Chris H Hill
  • Jack W Houghton
  • Md Firoz Ahmed
  • Robin Antrobus
  • Dmitri I Svergun
  • John J Welch
  • Colin M Crump
  • Stephen C Graham


Publication details

DateAccepted/In press - 7 May 2020
DatePublished (current) - 11 May 2020
Number of pages30
Original languageEnglish


Herpesviruses acquire their membrane envelopes in the cytoplasm of infected cells via a molecular mechanism that remains unclear. Herpes simplex virus (HSV)-1 proteins pUL7 and pUL51 form a complex required for efficient virus envelopment. We show that interaction between homologues of pUL7 and pUL51 is conserved across human herpesviruses, as is their association with trans-Golgi membranes. We characterized the HSV-1 pUL7:pUL51 complex by solution scattering and chemical crosslinking, revealing a 1:2 complex that can form higher-order oligomers in solution, and we solved the crystal structure of the core pUL7:pUL51 heterodimer. While pUL7 adopts a previously-unseen compact fold, the helix-turn-helix conformation of pUL51 resembles the cellular endosomal complex required for transport (ESCRT)-III component CHMP4B and pUL51 forms ESCRT-III-like filaments, suggesting a direct role for pUL51 in promoting membrane scission during virus assembly. Our results provide a structural framework for understanding the role of the conserved pUL7:pUL51 complex in herpesvirus assembly.

Bibliographical note

© 2020, Butt et al.

    Research areas

  • HEK293 Cells, HeLa Cells, Herpes Simplex/virology, Herpesvirus 1, Human/chemistry, Humans, Models, Molecular, Phosphoproteins/chemistry, Protein Binding, Protein Interaction Domains and Motifs, Protein Structure, Quaternary, Protein Structure, Tertiary, Viral Matrix Proteins/chemistry, Viral Proteins/chemistry, Virus Assembly, Virus Replication, trans-Golgi Network

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