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

DOI: 10.7554/eLife.53789 DOI Help

Authors: Benjamin G. Butt (University of Cambridge) , Danielle J. Owen (University of Cambridge) , C. M. Jeffries (European Molecular Biology Laboratory) , Lyudmila Ivanova (University of Cambridge) , Chris H. Hill (University of Cambridge) , Jack W. Houghton (University of Cambridge) , Md Firoz Ahmed (University of Cambridge) , Robin Antrobus (University of Cambridge) , Dmitri I. Svergun (European Molecular Biology Laboratory) , John J. Welch (University of Cambridge) , Colin M. Crump (University of Cambridge) , Stephen C. Graham (University of Cambridge)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Elife , VOL 9

State: Published (Approved)
Published: May 2020
Diamond Proposal Number(s): 15916

Open Access Open Access

Abstract: 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-IIIā€“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.

Journal Keywords: Small-angle X-ray scattering (SAXS); Secondary envelopment; virus budding; focal 23 adhesions; human cytomegalovirus (HCMV)

Diamond Keywords: Herpes; Viruses

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Added On: 20/05/2020 09:10

Discipline Tags:

Life Sciences & Biotech Biophysics Health & Wellbeing Infectious Diseases Pathogens Structural biology Chemistry Biochemistry

Technical Tags:

Diffraction Macromolecular Crystallography (MX)