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

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-IIIālike 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:
Pathogens
Infectious Diseases
Health & Wellbeing
Biochemistry
Chemistry
Structural biology
Biophysics
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)