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| Title | Open and closed forms of assembled henipavirus nucleoprotein suggest structural basis of genome access. |
|---|---|
| Journal, issue, pages | Sci Adv, Vol. 12, Issue 20, Page eaed8300, Year 2026 |
| Publish date | May 15, 2026 |
Authors | Rupesh Balaji Jayachandran / Erwan Quignon / Max Renner / ![]() |
| PubMed Abstract | Henipaviruses, such as Nipah virus, can cause deadly illness and constitute WHO blueprint priorities due to their pandemic potential. Their genomes are packaged within a nucleocapsid consisting of ...Henipaviruses, such as Nipah virus, can cause deadly illness and constitute WHO blueprint priorities due to their pandemic potential. Their genomes are packaged within a nucleocapsid consisting of viral nucleoproteins (N). Now, it is unclear how the encapsidated genome is released from N to allow the viral polymerase to read its sequence. Here, we present the high-resolution cryo-EM structure of a helical N-RNA filament from Langya henipavirus (LayV), allowing us to identify vertical interactions crucial for assembly. We show that assembly efficiency is sequence-dependent and prefers 5'-genomic sequences. Further, we solve the structure of an RNA-free assembly of LayV-N. Structural comparison of the RNA-bound and RNA-free LayV-N shows a conformational opening and closing, even within the assembled state. Our data suggest that N within nucleocapsids may undergo local conformational changes, switching between closed and open states, to temporarily allow access to the encapsidated RNA without nucleocapsid disruption. |
External links | Sci Adv / PubMed:42127178 / PubMed Central |
| Methods | EM (single particle) / EM (helical sym.) |
| Resolution | 2.6 - 3.1 Å |
| Structure data | EMDB-55586, PDB-9t5k: EMDB-55587, PDB-9t5l: ![]() EMDB-55588: Langya henipavirus Ncore 13mer Ring |
| Source |
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Keywords | VIRAL PROTEIN / Henipavirus / Langya virus / cryo-EM / nucleocapsid / nucleoprotein / RNA |
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