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TitleConserved assembly architecture of the essential herpesvirus packaging accessory factor.
Journal, issue, pagesBiorxiv, Year 2026
Publish dateDec 9, 2025 (structure data deposition date)
AuthorsElizabeth J Bailey / Swapnil C Devarkar / Renata Szczepaniak / Laura M Meißner / Xinyu Chen / Chunxiang Wu / Sandra K Weller / Yong Xiong / Allison L Didychuk /
PubMed AbstractTo create a new wave of infectious virions, all herpesviruses require an accessory factor of unknown function to package their viral genomes into nascent capsids. Here, we present cryo-EM structures ...To create a new wave of infectious virions, all herpesviruses require an accessory factor of unknown function to package their viral genomes into nascent capsids. Here, we present cryo-EM structures of the packaging accessory factor from the α-herpesvirus herpes simplex virus type 1 (HSV-1, UL32) and the β-herpesvirus human cytomegalovirus (HCMV, UL52). Unlike homologs from the γ-herpesviruses, neither UL32 nor UL52 form stable homopentameric rings. UL52 forms incomplete pentameric rings lacking one or two protomers. UL32 does not form stable higher-order species, but stabilization through chemical crosslinking revealed a novel quaternary structure where three pentameric rings assemble into a "tripentamer." Our results reveal that herpesvirus packaging accessory factors adopt distinct oligomeric states but are constrained to pentameric symmetry. Assembly of protomers into a ring creates a positively charged central channel that we show is critical for infectious virus production in HSV-1. Taken together, our study points to a structurally conserved, essential function of packaging accessory factors across the .
External linksBiorxiv / PubMed:41648366 / PubMed Central
MethodsEM (single particle)
Resolution3.07 - 3.29 Å
Structure data

PDB-9zly:
HSV-1 UL32 tripentamer
Method: ELECTRON MICROSCOPY / Resolution: 3.07 Å

PDB-9zm2:
Human cytomegalovirus UL52 4-mer
Method: ELECTRON MICROSCOPY / Resolution: 3.29 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • human alphaherpesvirus 1 strain 17
  • human betaherpesvirus 5
KeywordsVIRAL PROTEIN / Herpes simplex virus type 1 / HSV-1 / viral genome packaging / packaging accessory factor / UL32 / Human cytomegalovirus / HCMV / UL52

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