Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex
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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.
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Funder: Nvidia; FundRef: http://dx.doi.org/10.13039/100007065
Funder: Wellcome Trust; FundRef: http://dx.doi.org/10.13039/100004440
Funder: John Lucas Walker Studentship
Funder: Commonwealth Scholarship Commission; FundRef: http://dx.doi.org/10.13039/501100000867
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Royal Society (098406/Z/12/B)