9T5K

Local refinement of RNA-free assembled Langya virus N-core

Summary for 9T5K

• Entry DOI: 10.2210/pdb9t5k/pdb
• EMDB information: 55586
• Descriptor: Nucleocapsid (1 entity in total)
• Functional Keywords: henipavirus, langya virus, cryo-em, nucleocapsid, nucleoprotein, rna, viral protein
• Biological source: Langya virus
• Total number of polymer chains: 1
• Total formula weight: 51199.47

Authors

Jayachandran, R.B.,Quignon, E.,Renner, M. (deposition date: 2025-11-05, release date: 2026-04-22, Last modification date: 2026-05-27)

Primary citation

Jayachandran, R.B.,Quignon, E.,Renner, M.
Open and closed forms of assembled henipavirus nucleoprotein suggest structural basis of genome access.
Sci Adv, 12:eaed8300-eaed8300, 2026

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 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.

PubMed: 42127178
DOI: 10.1126/sciadv.aed8300

Experimental method

ELECTRON MICROSCOPY (2.6 Å)