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

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Owen, Danielle J 
Jeffries, Cy M 
Ivanova, Lyudmila 


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.



focal adhesions, human cytomegalovirus (hcmv), infectious disease, microbiology, molecular biophysics, secondary envelopment, small-angle X-ray scattering (SAXS), structural biology, virus, virus budding, HEK293 Cells, HeLa Cells, Herpes Simplex, Herpesvirus 1, Human, Humans, Models, Molecular, Phosphoproteins, Protein Binding, Protein Interaction Domains and Motifs, Protein Structure, Quaternary, Protein Structure, Tertiary, Viral Matrix Proteins, Viral Proteins, Virus Assembly, Virus Replication, trans-Golgi Network

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eLife Sciences Publications, Ltd


All rights reserved
Wellcome Trust (098406/Z/12/B)
Wellcome Trust (098406/Z/12/Z)
Remote synchrotron access was supported in part by the EU FP7 infrastructure grant BIOSTRUCT-X (Contract No. 283570) and access to P12 was supported by iNEXT funded by the Horizon 2020 programme of the European Commission (grant number 653706). A Titan V graphics card used for this research was donated by the NVIDIA Corporation. BGB is a Wellcome Trust PhD student, DJO was supported by a John Lucas Walker Studentship, and MFA was supported by Commonwealth Scholarship Commission PhD scholarship (BDCA801 2014-7). This work was supported by a Sir Henry Dale Fellowship (098406/Z/12/B), jointly funded by the Wellcome Trust and the Royal Society (to SCG).
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