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| Title | Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers. |
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| Journal, issue, pages | Nat Commun, Vol. 15, Issue 1, Page 2256, Year 2024 |
| Publish date | Mar 13, 2024 |
 Authors | Quentin Durieux Trouilleton / Dominique Housset / Paco Tarillon / Benoît Arragain / Hélène Malet /  |
| PubMed Abstract | Hantaan virus is a dangerous human pathogen whose segmented negative-stranded RNA genome is replicated and transcribed by a virally-encoded multi-functional polymerase. Here we describe the complete ...Hantaan virus is a dangerous human pathogen whose segmented negative-stranded RNA genome is replicated and transcribed by a virally-encoded multi-functional polymerase. Here we describe the complete cryo-electron microscopy structure of Hantaan virus polymerase in several oligomeric forms. Apo polymerase protomers can adopt two drastically different conformations, which assemble into two distinct symmetric homodimers, that can themselves gather to form hexamers. Polymerase dimerization induces the stabilization of most polymerase domains, including the C-terminal domain that contributes the most to dimer's interface, along with a lariat region that participates to the polymerase steadying. Binding to viral RNA induces significant conformational changes resulting in symmetric oligomer disruption and polymerase activation, suggesting the possible involvement of apo multimers as protecting systems that would stabilize the otherwise flexible C-terminal domains. Overall, these results provide insights into the multimerization capability of Hantavirus polymerase and may help to define antiviral compounds to counteract these life-threatening viruses. |
 External links | Nat Commun / PubMed:38480734 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.6 - 3.6 Å |
| Structure data | EMDB-18343, PDB-8qe5: EMDB-18390, PDB-8qgt: EMDB-18391: Chimeric map of apo Hantaan virus polymerase in dimeric state  EMDB-18392: Hantaan virus polymerase Apo Dimer  EMDB-18393: Focused map used to visualize the endonuclease of Hantaan virus polymerase apo dimer  EMDB-18394: Focused map of Hantaan virus polymerase dimer used to refine the cap-binding domain EMDB-18397, PDB-8qh3:  EMDB-18405: Cryo-EM map focused on the external protomers and one internal protomer of Hantaan virus polymerase hexamer  EMDB-18406: Cryo-EM of Hantaan virus polymerase in hexameric state EMDB-18408: Chimeric cryo-EM map of Hantaan virus polymerase in hexameric state |
| Chemicals |  ChemComp-MG: |
| Source |
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 Keywords |  VIRAL PROTEIN / Bunyavirus / Hantaan virus / polymerase / dimer |
