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TitleRNA synthesis and substrate analogue inhibition in the CCHFV polymerase.
Journal, issue, pagesNature, Year 2026
Publish dateJul 22, 2026
AuthorsHengxia Jia / Bo Tang / Shunli Liu / Xin Wen / Fan Wu / Xiao Hu / Hu Zhou / Tingting Chong / Lincan Lv / Qiaojie Liu / Guibo Rao / Mingyu Wei / Xuping Jing / Sheng Cao / Fei Deng / Zhihong Hu / Bo Shu / Rui Gong / Jiqin Wu / Manli Wang / Peng Gong /
PubMed AbstractThe about 4,000-residue L proteins from the Nairoviridae are the largest known viral polymerases, lacking global structural information and promising nucleotide analogue inhibitors. Here we report ...The about 4,000-residue L proteins from the Nairoviridae are the largest known viral polymerases, lacking global structural information and promising nucleotide analogue inhibitors. Here we report structures of full-length Nairoviridae Crimean-Congo haemorrhagic fever virus (CCHFV) L, including a 3.0 Å resolution polymerase elongation complex that elucidates mechanisms of both early and late elongation stages. Large additions and insertions are found in all three major functional regions that contain the endonuclease RNA-dependent RNA polymerase (RdRP) and cap-binding domain of CCHFV L, extending RNA-binding paths on both sides of the RdRP active site and creating interaction networks critical for viral replication, as suggested by CCHFV minigenome assay data. Nucleotide analogues with ribose-2' modifications identical to the hepatitis C drug sofosbuvir are found to specifically and efficiently inhibit CCHFV RdRP through an immediate chain termination mechanism. Using a sofosbuvir-hepatitis C virus RdRP system as the reference, the potency of these nucleotide analogues is further demonstrated in competition assays in the presence of corresponding nucleoside triphosphates.
External linksNature / PubMed:42649282
MethodsEM (single particle)
Resolution2.67 - 3.18 Å
Structure data

80447

25xl

EMDB-80447, PDB-25xl:
Cryo-EM structure of the Crimean-Congo hemorrhagic fever virus L protein (apo form)
Method: EM (single particle) / Resolution: 2.88 Å

80448

25xm

EMDB-80448, PDB-25xm:
Cryo-EM structure of the Crimean-Congo hemorrhagic fever virus L protein (5'-cRNA-bound form)
Method: EM (single particle) / Resolution: 2.67 Å

80449

25xn

EMDB-80449, PDB-25xn:
Cryo-EM structure of the Crimean-Congo hemorrhagic fever virus full-length L protein RdRP elongation complex (EC14 form)
Method: EM (single particle) / Resolution: 3.01 Å

80450

25xo

EMDB-80450, PDB-25xo:
Cryo-EM structure of the Crimean-Congo hemorrhagic fever virus full-length L protein RdRP elongation complex (EC14b form)
Method: EM (single particle) / Resolution: 3.18 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MN:
Unknown entry

Source
  • orthonairovirus haemorrhagiae
  • synthetic construct (others)
KeywordsVIRAL PROTEIN / negative-strand RNA virus / Crimean-Congo hemorrhagic fever virus / RNA-dependent RNA polymerase / replication / transcription / VIRAL PROTEIN/RNA / transcription/RNA / REPLICATION-RNA complex / VIRAL PROTEIN-RNA complex / elongation complex

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