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TitleDouble-ring assembly of mpox virus I3L reveals an unconventional mechanism for ssDNA engagement.
Journal, issue, pagesCell Rep, Vol. 45, Issue 7, Page 117659, Year 2026
Publish dateJul 28, 2026
AuthorsKankan Yang / Mengrui Ge / Jinmiao Song / Junwei Zou / Yingying Zhang / Haiqiang Wu / Yong Wang / Jun Ma /
PubMed AbstractPoxviruses, including variola and mpox virus (MPXV), are large dsDNA viruses that replicate their genomes in the host cytoplasm via virally encoded proteins. The single-stranded DNA-binding protein ...Poxviruses, including variola and mpox virus (MPXV), are large dsDNA viruses that replicate their genomes in the host cytoplasm via virally encoded proteins. The single-stranded DNA-binding protein (SSB) I3L is an essential component of this replication machinery, yet its structural mechanism remains to be fully elucidated. Here, we determined the cryo-EM structure of MPXV I3L and constructed a structural model of its complex with ssDNA. Unlike canonical SSBs, I3L forms an architectural double-ring assembly. The individual I3L protomer adopts an OB-fold variant with specialized elements beyond the classic pattern. Furthermore, biochemical assays and structural modeling suggest an assembly-dependent ssDNA-engagement mode, while monomeric binding features remain conserved. These distinctive structural features suggest a specialized molecular mechanism for poxviral DNA replication. Our findings advance the mechanistic understanding of poxvirus genome maintenance and provide perspectives for antiviral development against MPXV.
External linksCell Rep / PubMed:42418326
MethodsEM (single particle)
Resolution3.6 Å
Structure data

65952

9wgb

EMDB-65952, PDB-9wgb:
Cryo-EM structure of I3L-ssDNA double-ring complex
Method: EM (single particle) / Resolution: 3.6 Å

Source
  • monkeypox virus zaire-96-i-16
KeywordsVIRAL PROTEIN / ssDNA-binding / DNA replication / double-ring complex / OB-like

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