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TitleStructural plasticity of mumps virus nucleocapsids with cryo-EM structures.
Journal, issue, pagesCommun Biol, Vol. 4, Issue 1, Page 833, Year 2021
Publish dateJul 2, 2021
AuthorsHong Shan / Xin Su / Tianhao Li / Yuqi Qin / Na Zhang / Liuyan Yang / Linsha Ma / Yun Bai / Lei Qi / Yunhui Liu / Qing-Tao Shen /
PubMed AbstractMumps virus (MuV) is a highly contagious human pathogen and frequently causes worldwide outbreaks despite available vaccines. Similar to other mononegaviruses such as Ebola and rabies, MuV uses a ...Mumps virus (MuV) is a highly contagious human pathogen and frequently causes worldwide outbreaks despite available vaccines. Similar to other mononegaviruses such as Ebola and rabies, MuV uses a single-stranded negative-sense RNA as its genome, which is enwrapped by viral nucleoproteins into the helical nucleocapsid. The nucleocapsid acts as a scaffold for genome condensation and as a template for RNA replication and transcription. Conformational changes in the MuV nucleocapsid are required to switch between different activities, but the underlying mechanism remains elusive due to the absence of high-resolution structures. Here, we report two MuV nucleoprotein-RNA rings with 13 and 14 protomers, one stacked-ring filament and two nucleocapsids with distinct helical pitches, in dense and hyperdense states, at near-atomic resolutions using cryo-electron microscopy. Structural analysis of these in vitro assemblies indicates that the C-terminal tail of MuV nucleoprotein likely regulates the assembly of helical nucleocapsids, and the C-terminal arm may be relevant for the transition between the dense and hyperdense states of helical nucleocapsids. Our results provide the molecular mechanism for structural plasticity among different MuV nucleocapsids and create a possible link between structural plasticity and genome condensation.
External linksCommun Biol / PubMed:34215847 / PubMed Central
MethodsEM (single particle) / EM (helical sym.)
Resolution2.9 - 3.9 Å
Structure data

EMDB-30281:
Structure of Mumps virus nuleocapcid ring
Method: EM (single particle) / Resolution: 3.2 Å

31361

7ewq

EMDB-31361, PDB-7ewq:
Structure of Mumps virus nucleocapsid ring
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-31367: Structure of mumps virus nucleoprotein without C-arm
Method: EM (helical sym.) / Resolution: 2.9 Å

EMDB-31368:
dense nucleocapsid of Mumps virus
Method: EM (helical sym.) / Resolution: 3.9 Å

EMDB-31369:
Structure of hyperdense Mumps virus nucleocapsid at 3.6 Angstroms resolution
Method: EM (helical sym.) / Resolution: 3.6 Å

EMDB-31370:
Structure of ring-stacked Mumps virus nucleocapsid filament
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • Mumps rubulavirus
  • mumps virus (strain jeryl-lynn)
  • mumps orthorubulavirus
  • Escherichia coli (E. coli)
KeywordsNUCLEAR PROTEIN / nucleocapcid / Mumps virus

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