Structure of herpes simplex virus pUL7:pUL51, a conserved complex required for efficient herpesvirus assembly

摘要: Abstract Herpesviruses are an ancient family of highly-prevalent human and animal pathogens that acquire their membrane envelopes in the cytoplasm infected cells. While multiple conserved viral proteins known to be required for efficient herpesvirus production, many these lack identifiable structural homologues molecular details assembly remain unclear. We have characterized complex pUL7 pUL51 from herpes simplex virus (HSV)-1, α-herpesvirus, using multi-angle light scattering small-angle X-ray with chemical crosslinking. HSV-1 form a stable 1:2 is capable higher-order oligomerization solution. solved crystal structure this complex, revealing core heterodimer comprising bound residues 41–125 pUL51. adopts previously-unseen compact fold, extended helix-turn-helix conformation resembles cellular endosomal transport (ESCRT)-III component CHMP4B, suggesting direct role promoting scission during assembly. demonstrate interaction between across α-, β- γ-herpesviruses, as association trans-Golgi membranes cultured However, do not complexes respective partners different families, interface diverged. Our results pUL7:pUL51 herpesviruses provide framework understanding its Significance Statement extremely common cause diseases ranging cold sores cancer. Herpesvirus envelope via pathway, which (HSV)-1 pUL51, two show formation distantly-related herpesviruses, used virion key membrane-remodeling components, may play deforming promote