8OP2

Stacks of nucleocapsid rings of the N1-370 mutant of the human Respiratory Syncytial Virus

Summary for 8OP2

• Entry DOI: 10.2210/pdb8op2/pdb
• EMDB information: 17030 17031 17034 17035 17036 17037 17038
• Descriptor: Nucleoprotein, RNA (70-mer) (2 entities in total)
• Functional Keywords: n-rna, nucleoprotein, nucleocapsid, rsv, viral protein
• Biological source: Human respiratory syncytial virus A strain Long; More
• Total number of polymer chains: 22
• Total formula weight: 864960.63

Authors

Gonnin, L.,Desfosses, A.,Gutsche, I. (deposition date: 2023-04-06, release date: 2023-09-27)

Primary citation

Gonnin, L.,Desfosses, A.,Bacia-Verloop, M.,Chevret, D.,Galloux, M.,Eleouet, J.F.,Gutsche, I.
Structural landscape of the respiratory syncytial virus nucleocapsids.
Nat Commun, 14:5732-5732, 2023

PubMed Abstract: Human Respiratory Syncytial Virus (HRSV) is a prevalent cause of severe respiratory infections in children and the elderly. The helical HRSV nucleocapsid is a template for the viral RNA synthesis and a scaffold for the virion assembly. This cryo-electron microscopy analysis reveals the non-canonical arrangement of the HRSV nucleocapsid helix, composed of 16 nucleoproteins per asymmetric unit, and the resulting systematic variations in the RNA accessibility. We demonstrate that this unique helical symmetry originates from longitudinal interactions by the C-terminal arm of the HRSV nucleoprotein. We explore the polymorphism of the nucleocapsid-like assemblies, report five structures of the full-length particles and two alternative arrangements formed by a C-terminally truncated nucleoprotein mutant, and demonstrate the functional importance of the identified longitudinal interfaces. We put all these findings in the context of the HRSV RNA synthesis machinery and delineate the structural basis for its further investigation.

PubMed: 37714861
DOI: 10.1038/s41467-023-41439-8

Experimental method

ELECTRON MICROSCOPY (2.8 Å)