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TitleCryo EM structure of the rabies virus ribonucleoprotein complex.
Journal, issue, pagesSci Rep, Vol. 9, Issue 1, Page 9639, Year 2019
Publish dateJul 3, 2019
AuthorsChristiane Riedel / Daven Vasishtan / Vojtěch Pražák / Alexander Ghanem / Karl-Klaus Conzelmann / Till Rümenapf /
PubMed AbstractRabies virus is an important zoonotic pathogen. Its bullet shaped particle contains a helical nucleocapsid. We used cryo-electron tomography and subsequent subtomogram averaging to determine the ...Rabies virus is an important zoonotic pathogen. Its bullet shaped particle contains a helical nucleocapsid. We used cryo-electron tomography and subsequent subtomogram averaging to determine the structure of its ribonucleoprotein. The resulting electron density map allowed for confident fitting of the N-protein crystal structure, indicating that interactions between neighbouring N-proteins are only mediated by N- and C-terminal protruding subdomains (aa 1-27 and aa 355-372). Additional connecting densities, likely stabilizing the ribonucleoprotein complex, are present between neighbouring M-protein densities on the same helical turn and between M- and N-protein densities located on neighbouring helical turns, but not between M-proteins of different turns, as is observed for the related Vesicular stomatitis virus (VSV). This insight into the architecture of the rabies virus nucleocapsid highlights the surprising structural divergence of large biological assemblies even if the building blocks - here exemplified by VSV M- and N-protein - are structurally closely related.
External linksSci Rep / PubMed:31270364 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution15.0 Å
Structure data

EMDB-4995:
Subtomogram average of a part of the rabies lyssavirus ribonucleoprotein
Method: EM (subtomogram averaging) / Resolution: 15.0 Å

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