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TitleStructure of the recombinant RNA polymerase from African Swine Fever Virus.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 1606, Year 2024
Publish dateFeb 21, 2024
AuthorsSimona Pilotto / Michal Sýkora / Gwenny Cackett / Christopher Dulson / Finn Werner /
PubMed AbstractAfrican Swine Fever Virus is a Nucleo-Cytoplasmic Large DNA Virus that causes an incurable haemorrhagic fever in pigs with a high impact on global food security. ASFV replicates in the cytoplasm of ...African Swine Fever Virus is a Nucleo-Cytoplasmic Large DNA Virus that causes an incurable haemorrhagic fever in pigs with a high impact on global food security. ASFV replicates in the cytoplasm of the infected cell and encodes its own transcription machinery that is independent of cellular factors, however, not much is known about how this system works at a molecular level. Here, we present methods to produce recombinant ASFV RNA polymerase, functional assays to screen for inhibitors, and high-resolution cryo-electron microscopy structures of the ASFV RNAP in different conformational states. The ASFV RNAP bears a striking resemblance to RNAPII with bona fide homologues of nine of its twelve subunits. Key differences include the fusion of the ASFV assembly platform subunits RPB3 and RPB11, and an unusual C-terminal domain of the stalk subunit vRPB7 that is related to the eukaryotic mRNA cap 2´-O-methyltransferase 1. Despite the high degree of structural conservation with cellular RNA polymerases, the ASFV RNAP is resistant to the inhibitors rifampicin and alpha-amanitin. The cryo-EM structures and fully recombinant RNAP system together provide an important tool for the design, development, and screening of antiviral drugs in a low biosafety containment environment.
External linksNat Commun / PubMed:38383525 / PubMed Central
MethodsEM (single particle)
Resolution2.69 - 2.99 Å
Structure data

18120

8q3b

EMDB-18120, PDB-8q3b:
The closed state of the ASFV apo-RNA polymerase
Method: EM (single particle) / Resolution: 2.69 Å

18129

8q3k

EMDB-18129, PDB-8q3k:
The open state of the ASFV apo-RNA polymerase
Method: EM (single particle) / Resolution: 2.92 Å

EMDB-18163: consensus map of the ASFV RNA polymerase in open conformation
Method: EM (single particle) / Resolution: 2.92 Å

EMDB-18164: The stalk domain of the ASFV RNA polymerase obtained from Multibody refinement
Method: EM (single particle) / Resolution: 2.99 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • african swine fever virus ba71v
KeywordsTRANSCRIPTION / RNA polymerase / ASFV / eukaryotic virus

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