Butt, Benjamin G, Owen, Danielle J, Jeffries, Cy M et al. (9 more authors) (2020) Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex. eLife. e53789. ISSN 2050-084X
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-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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2020, Butt et al. |
Keywords: | 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 |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) |
Depositing User: | Pure (York) |
Date Deposited: | 22 Oct 2021 10:50 |
Last Modified: | 21 Jan 2025 17:57 |
Published Version: | https://doi.org/10.7554/eLife.53789 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.7554/eLife.53789 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:179527 |
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Filename: elife_53789_v3.pdf
Description: Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex
Licence: CC-BY 2.5