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

Benjamin G Butt, Danielle J Owen, Cy M Jeffries, Lyudmila Ivanova, Chris H Hill, Jack W Houghton, Md Firoz Ahmed, Robin Antrobus, Dmitri I Svergun, John J Welch, Colin M Crump, Stephen C Graham

eLife 2020 May 11

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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. © 2020, Butt et al.

Citation

Benjamin G Butt, Danielle J Owen, Cy M Jeffries, Lyudmila Ivanova, Chris H Hill, Jack W Houghton, Md Firoz Ahmed, Robin Antrobus, Dmitri I Svergun, John J Welch, Colin M Crump, Stephen C Graham. Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex. eLife. 2020 May 11;9