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TitleAsymmetric reconstruction of mammalian reovirus reveals interactions among RNA, transcriptional factor µ2 and capsid proteins.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 4176, Year 2021
Publish dateJul 7, 2021
AuthorsMuchen Pan / Ana L Alvarez-Cabrera / Joon S Kang / Lihua Wang / Chunhai Fan / Z Hong Zhou /
PubMed AbstractMammalian reovirus (MRV) is the prototypical member of genus Orthoreovirus of family Reoviridae. However, lacking high-resolution structures of its RNA polymerase cofactor μ2 and infectious ...Mammalian reovirus (MRV) is the prototypical member of genus Orthoreovirus of family Reoviridae. However, lacking high-resolution structures of its RNA polymerase cofactor μ2 and infectious particle, limits understanding of molecular interactions among proteins and RNA, and their contributions to virion assembly and RNA transcription. Here, we report the 3.3 Å-resolution asymmetric reconstruction of transcribing MRV and in situ atomic models of its capsid proteins, the asymmetrically attached RNA-dependent RNA polymerase (RdRp) λ3, and RdRp-bound nucleoside triphosphatase μ2 with a unique RNA-binding domain. We reveal molecular interactions among virion proteins and genomic and messenger RNA. Polymerase complexes in three Spinoreovirinae subfamily members are organized with different pseudo-D symmetries to engage their highly diversified genomes. The above interactions and those between symmetry-mismatched receptor-binding σ1 trimers and RNA-capping λ2 pentamers balance competing needs of capsid assembly, external protein removal, and allosteric triggering of endogenous RNA transcription, before, during and after infection, respectively.
External linksNat Commun / PubMed:34234134 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 8.6 Å
Structure data

EMDB-31183, PDB-7elh:
In situ structure of transcriptional enzyme complex and capsid shell protein of mammalian reovirus at initiation state
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-31184, PDB-7ell:
In situ structure of capping enzyme lambda2, penetration protein mu1 of mammalian reovirus capsid asymmetric unit.
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-31187:
Asymmetric ISVP of Mammalian reovirus 3
Method: EM (single particle) / Resolution: 4.6 Å

EMDB-31188:
Icosahedral ISVP
Method: EM (single particle) / Resolution: 8.6 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION / Phosphate

ChemComp-MYR:
MYRISTIC ACID / Myristic acid

Source
  • mammalian orthoreovirus 3
  • mammalian orthoreovirus 3 dearing
KeywordsVIRAL PROTEIN/TRANSFERASE/RNA / asymmetric / mu2 / lambda3 / lambda1 / VIRUS / VIRAL PROTEIN-TRANSFERASE-RNA complex / VIRAL PROTEIN/TRANSFERASE / mammalian reovirus 3 / capping enzyme lambda2 / penetration protein mu1 / VIRAL PROTEIN-TRANSFERASE complex

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