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TitleStructure of the Ebola virus polymerase complex.
Journal, issue, pagesNature, Vol. 610, Issue 7931, Page 394-401, Year 2022
Publish dateSep 28, 2022
AuthorsBin Yuan / Qi Peng / Jinlong Cheng / Min Wang / Jin Zhong / Jianxun Qi / George F Gao / Yi Shi /
PubMed AbstractFiloviruses, including Ebola virus, pose an increasing threat to the public health. Although two therapeutic monoclonal antibodies have been approved to treat the Ebola virus disease, there are no ...Filoviruses, including Ebola virus, pose an increasing threat to the public health. Although two therapeutic monoclonal antibodies have been approved to treat the Ebola virus disease, there are no approved broadly reactive drugs to control diverse filovirus infection. Filovirus has a large polymerase (L) protein and the cofactor viral protein 35 (VP35), which constitute the basic functional unit responsible for virus genome RNA synthesis. Owing to its conservation, the L-VP35 polymerase complex is a promising target for broadly reactive antiviral drugs. Here we determined the structure of Ebola virus L protein in complex with tetrameric VP35 using cryo-electron microscopy (state 1). Structural analysis revealed that Ebola virus L possesses a filovirus-specific insertion element that is essential for RNA synthesis, and that VP35 interacts extensively with the N-terminal region of L by three protomers of the VP35 tetramer. Notably, we captured the complex structure in a second conformation with the unambiguous priming loop and supporting helix away from polymerase active site (state 2). Moreover, we demonstrated that the century-old drug suramin could inhibit the activity of the Ebola virus polymerase in an enzymatic assay. The structure of the L-VP35-suramin complex reveals that suramin can bind at the highly conserved NTP entry channel to prevent substrates from entering the active site. These findings reveal the mechanism of Ebola virus replication and may guide the development of more powerful anti-filovirus drugs.
External linksNature / PubMed:36171293 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 3.4 Å
Structure data

33775

7yer

EMDB-33775, PDB-7yer:
The structure of EBOV L-VP35 complex
Method: EM (single particle) / Resolution: 3.0 Å

33776

7yes

EMDB-33776, PDB-7yes:
The structure of EBOV L-VP35-RNA complex (state2)
Method: EM (single particle) / Resolution: 3.4 Å

33777

7yet

EMDB-33777, PDB-7yet:
The structure of EBOV L-VP35 in complex with suramin
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SVR:
8,8'-[CARBONYLBIS[IMINO-3,1-PHENYLENECARBONYLIMINO(4-METHYL-3,1-PHENYLENE)CARBONYLIMINO]]BIS-1,3,5-NAPHTHALENETRISULFON / medication*YM

Source
  • ebola virus
KeywordsVIRAL PROTEIN / polymerase / complex

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