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

eLife

Jack W Houghton¹  Robin Antrobus¹  John J Welch²  Lyudmila Ivanova³  Md Firoz Ahmed³  Colin M Crump³  Danielle J Owen³  Benjamin G Butt³  Stephen C Graham³  Chris H Hill³  Dmitri I Svergun⁴  Cy M Jeffries⁴ 

[1] Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom;Department of Genetics, University of Cambridge, Cambridge, United Kingdom;Department of Pathology, University of Cambridge, Cambridge, United Kingdom;European Molecular Biology Laboratory (EMBL) Hamburg Site, Hamburg, Germany;

关键词: small-angle X-ray scattering (SAXS);    secondary envelopment;    virus budding;    focal adhesions;    human cytomegalovirus (hcmv);   

DOI  :  10.7554/eLife.53789

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown